Atomic structure of the catalytic domain for use in designing and identifying inhibitors of zap-70 kinase

ABSTRACT

The present invention relates to the three dimensional structure of ZAP-70 protein tyrosine kinase and describes methods of making a crystal of ZAP-70 and purification of the catalytic domain of ZAP-70 for use in crystallization. The invention also relates to the use of the three dimensional structure of the catalytic domain of ZAP-70 for identifying and designing ligands which inhibit the biological function of ZAP-70.

FIELD OF THE INVENTION

The present invention relates to ZAP-70 protein tyrosine kinase, inparticular, the three-dimensional structure of the catalytic domain ofZAP-70 protein tyrosine kinase. The invention also relates to thecrystalline forms of liganded or unliganded human ZAP-70 catalyticdomain. Further, the invention describes methods of making of a crystalcomprising ZAP-70 and purification of the catalytic domain of ZAP-70 foruse in crystallization. The invention also relates to the use of thethree-dimensional structure of the catalytic domain of ZAP-70 kinase foridentifying and designing ligands or low molecular weight compoundswhich inhibit the biological function of ZAP-70.

BACKGROUND OF THE INVENTION

The protein tyrosine kinase ZAP-70 (zeta chain-associated protein of 70kDa) plays a pivotal role in T cell activation. T cells are involved intransplant rejection, autoimmune diseases and the initiation ofinflammatory responses. Activation of T cells requires engagement of theantigen-specific T cell receptor (TCR), resulting in early membraneproximal events which lead to the activation of a number of signaltransduction pathways.

One of the early events of T cell activation is the phosphorylation ofthe TCR zeta chain and the specific association and activation of theSyk family protein tyrosine kinase ZAP-70 with the TCR via its two SH2domains. Zeta chain-binding together with trans-phosphorylation by thesrc family kinase Lck leads to the activation of ZAP-70. ZAP-70phosphorylates its specific substrate LAT (linker for activation of Tcells), an adaptor molecule, which then recruits a number of downstreameffector molecules. This eventually leads to the activation of early Tcell genes, production of cytokines and cellular proliferation. There isample evidence that interference with ZAP-70/LAT-mediated signalingleads to functional T cell inactivation.

Defects in ZAP-70 are the cause of selective T cell defect (STD), anautosomal recessive form of severe combined immunodeficiencycharacterized by a selective absence of CD-8-type T cells.

The crystal structure of the tandem SH2 domains of human ZAP-70 incomplex with a peptide derived from the TCR zeta chain has beenpreviously described by Hatada et al. (1995). This three-dimensionalcrystal structure of the SH2 domain has also been the subject of U.S.Pat. No. 6,251,620. The disclosure of this SH2 domain has lead toefforts directed at blocking the ZAP-70 SH2 domain/zeta chaininteraction. However, to date no orally active inhibitor of ZAP-70 hasbeen described.

The present invention focuses on the three dimensional structure of thecatalytic domain of ZAP-70 for inhibition of ZAP-70 since catalyticactivity at the ATP-binding site can be directly inhibited. Before thedisclosure of the present invention, there was no three-dimensionalcrystal structure of the catalytic domain of ZAP-70. With thethree-dimensional structure of the catalytic domain of the human ZAP-70,identifying and designing inhibitors of ZAP-70 based on thethree-dimensional structure of the catalytic domain is now possible.

SUMMARY OF THE INVENTION

It is an object of the present invention to provide thethree-dimensional structure of ZAP-70 kinase catalytic domain therebyenabling identification and design of ligands or low molecular weightmolecules that specifically inhibit ZAP-70 kinase.

The present invention relates to:

(i) a crystal of the ZAP-70 kinase comprising the catalytic domain ofZAP-70 kinase with or without a ligand or low molecular weight compound

(ii) a method of making a crystal of ZAP-70 kinase comprising the ZAP-70kinase catalytic domain

(iii) methods of using said ZAP-70 kinase crystal comprising thecatalytic domain and its structural coordinates.

The three-dimensional structural information revealed from the crystalof the the catalytic domain of ZAP-70 kinase can be used forstructure-based drug discovery for screening, identifying and designinginhibitors of ZAP-70 kinase.

DETAILED DESCRIPTION OF THE INVENTION

The full-length sequence of human ZAP-70 kinase is known and set forthin Genbank Accession number L05148 and SwissProt Accession numberP43403, which are incorporated herein by reference.

The present invention provides ZAP-70 kinase catalytic domain incrystallized form. In particular, it provides a crystal comprising thecatalytic domain of ZAP-70 kinase and a ligand bound to ZAP-70 as acomplex.

In one embodiment of the present invention, a crystal of the catalyticdomain of ZAP-70 kinase comprising a unit cell dimension of a=35.77±5Ångstroms b=57.56±5 Ångstroms c=80.20±5 Ångstroms, α=68.97±5 degreesβ=89.83±5 degrees γ=89.95±5 degrees is provided. Depending on theparticular conditions for crystallization, the parameters characterisingthe unit cell may vary with a limited range, for example, a, b, c eachvary by up to 5 Angstroms and α, β, γ each vary by up to 5 degrees. Thespace group of the present invention is P1 primitive triclinic.

The term “unit cell” according to the invention refers to the basicshape block. The entire volume of a crystal may be constructed byregular assembly of such blocks. Each unit cell comprises a completerepresentation of the unit of pattern, the repetition of which builds upthe crystal.

The term “space group” according to the invention refers to thearrangement of symmetry elements of a crystal.

In another embodiment of the invention, a crystal of ZAP-70 kinasecomprising the catalytic domain of ZAP-70 kinase in complex with aligand is provided wherein said crystal has a three-dimensionalstructure characterized by the atomic structure coordinates of Table 1.

In a further embodiment of the invention, said catalytic domain ofZAP-70 kinase comprises the sequence of SEQ ID. No. 2, fragment orhomologue thereof.

In yet another embodiment of the invention, said catalytic domain ofZAP-70 kinase comprises at least the ATP-binding site.

Further provided by this invention is a crystal comprising the catalyticdomain of ZAP-70 bound to at least one ligand or low molecular weightcompound.

The term “ligand” according to the invention, refers to a molecule orgroup of molecules that bind to one or more specific sites of ZAP-70,preferably to the catalytic domain of ZAP-70 and most preferably to theATP binding-site of said catalytic domain. Ligands according to theinvention are preferably low molecular weight molecules.

The term “low molecular weight compound” according to the inventionrefers to preferably organic compounds generally having a molecularweight less than about 1000, more preferably less than about 500. Mostpreferably, said low molecular weight compounds or ligands inhibitZAP-70 biological activity.

In context of a ZAP-70 inhibitor, the terms “peptide” or “peptidederivative” are intended to embrace a “peptidomimetic” or “peptideanalogue” which complement the three-dimensional structure of thebinding site of ZAP-70 kinase or can be designed with improved physicalor chemical properties to bind with the three-dimensional binding siteof the ZAP-70 kinase catalytic domain as provided in the presentinvention.

The term “mutant” refers to differences in the wild-type sequence ofZAP-70 kinase set forth in Genbank Accession number L05148 or SwissProtAccession number P43403 by deletion, insertion or preferably replacementof one or more selected amino acids.

According to the present invention, the term “mutant” also refers to apolypeptide, whose amino acid sequence differs from the wild-typesequence given in SEQ ID No.2 by deletion, insertion or preferablyreplacement of one or more selected amino acids. For example, a ZAP-70mutant of the catalytic domain of the present invention is preferably atleast 50% homologous to SEQ ID No. 2, more preferably at least 80%homologous to SEQ ID No. 2 most preferably at least 90% homologous toSEQ ID No. 2.

A “fragment” of ZAP-70 catalytic domain according to the inventioncomprises more than 50% of the full-length sequence of the ZAP-70catalytic domain according to SEQ ID No. 2, more preferably at least 80%of the full-length sequence of the ZAP-70 catalytic domain according toSEQ ID No. 2, most preferably at least 90% of the full-length sequenceof the ZAP-70 catalytic domain according to SEQ ID No. 2.

In one embodiment of the invention, a ZAP-70 mutant of the catalyticdomain may be crystallizable with or without at least one ligand.

In another embodiment of the invention, a ZAP-70 fragment of thecatalytic domain may be crystallizable with or without at least oneligand.

In yet another embodiment of the invention, a method is provided whereinthe catalytic domain of ZAP-70, a fragment or homologue thereof is boundto at least one ligand at any step prior to crystallization.

According to the present invention, ZAP-70 crystals are stable for atleast one month, if kept under suitable conditions. Hepes pH 7.2 isidentified as being suitable for the concentration of ZAP-70 withoutprecipitation. Initially during purification, high concentrations ofglycerol (30-50% v/v) are preferred, below which rapid precipitationoccurs at protein concentrations in excess of 5-10 mg/ml. During thefinal concentration steps 1% v/v ethylene glycol can substitute forglycerol allowing concentrations in excess of 30 mg/ml to be reached. Anadditional cation-exchange step is also recommended to removeincorrectly folded or unstable ZAP-70 which interferes with theconcentration and crystallisation process.

The purified protein ZAP-70 catalytic domain of SEQ. ID No.2, homologueor fragment thereof is advantageously obtainable according to method ofthe present invention by initial expression of the full-length ZAP-70SEQ ID No.1 flanked by protease recognition sequences. This facilitatesefficient proteolytic release of the desired domain. This method ispreferable to standard methods known in the art whereby the desireddomain typically is isolated from the full-length protein and thenexpressed.

Purification of an N-terminally tagged full-length ZAP-70 using anickel-chelating affinity column yields protein of limited purity whichcannot be easily purified by additional “standard” chromatographicprocedures such as ion-exchange or size-exclusion chromatography.According to the present invention, affinity chromatography usingγ-aminophenyl-ATP sepharose is the preferred means of purificationleading to a high purity the ZAP-70 protein. Identification of thedesired ZAP-70 catalytic domain is preferably by immunochemical method,for example, Western-blotting.

In one embodiment of the invention, a method for making a crystal of aZAP-70 kinase is provided comprising the following steps:

(i) purification of the full-length ZAP-70 kinase (SEQ ID No.1)

(ii) proteolytic domain definition

(iii) expression of the full-length ZAP-70 kinase of SEQ ID No.1 flankedby protease recognition sequences to facilitate proteolytic release ofthe desired domain of ZAP-70

(iv) expression of the full-length ZAP-kinase from step (iii) in asuitable host cell

(v) controlled proteolysis of the desired domain at protease recognitionsites

(vi) rapid purification of the desired ZAP-70 domain.

In a preferred embodiment of the invention, said method for making acrystal comprises the desired domain of ZAP-70 kinase domain comprisingthe catalytic domain of ZAP-70 kinase of SEQ ID No.2, a fragment orhomologue thereof.

According to the invention, ZAP-70 may be prepared by isolation fromnatural sources, e.g. cultured human cells or preferably by recombinantheterologous expression. Expression of recombinant ZAP-70 is achievablein eukaryotic or prokaryotic systems. For example, recombinant humanZAP-70 may be expressed in insect cells, such as Sf9 cells, using asuitable recombinant baculovirus system or in bacteria.

The kinase may be expressed as a fusion protein, e.g. aglutathione-S-transferase (GST) or histidine-tagged fusion protein. Ifdesired, the fusion partner is removed before crystallization. Theheterologously produced ZAP-70 to be used for crystallization isbiologically active. Such ability may be determined by morphological,biochemical or viability analysis well-known in the art.

Methods for the preparation of ZAP-70 mutants are commonly known in theart. For example, ZAP-70 mutants may be prepared by expression of ZAP-70DNA previously modified in its coding region by oligo-nucleotidedirected mutagenesis.

In the present invention, purified ZAP-70 is preferably at least 90%homogeneous. Protein homogeneity is determinable according to analyticalmethods well-known in the art, e.g. sequence analysis, electrophoresis,spectroscopic or chromatographic techniques. The purified protein isenzymatically active. Appropriate assays for determining ZAP-70 kinaseactivity towards a suitable substrate, e.g. a natural substrate or asynthetic substrate which is known in the art.

In one embodiment of the invention, prior to crystallization ZAP-70 maybe reacted with a low molecular weight compound or ligand which iscapable of suitably binding to the ZAP-70 catalytic domain site.Preferred is a compound inhibiting ZAP-70 activity. Kinase inhibition isdeterminable employing assays known in the art. Suitable inhibitorsinclude ATP-competitive kinase inhibitors which act on the catalyticdomain to inhibit ZAP-70 activity.

Various methods of cystallization can be used in the claimed inventionincluding vapor diffusion, dialysis or batch crystallization. In vapordiffusion crystallization, a small volume (i.e., a few microliters) ofprotein solution is mixed with a solution containing a precipitant. Thismixed volume is suspended over a well containing a small amount, i.e.about 1 ml, of precipitant. Vapor diffusion from the drop to the wellwill result in crystal formation in the drop.

The dialysis method of crystallization utilizes a semipermeablesize-exclusion membrane that retains the protein but allows smallmolecules (i.e. buffers and precipitants) to diffuse in and out. Indialysis, rather than concentrating the protein and the precipitant byevaporation, the precipitant is allowed to slowly diffuse through themembrane and reduce the solubility of the protein while keeping theprotein concentration fixed.

The batch method generally involves the slow addition of a precipitantto an aqueous solution of protein until the solution just becomesturbid, at this point the container can be sealed and left undisturbedfor a period of time until crystallization occurs. In the batchtechnique the precipitant and the target molecule solution are simplymixed. Supersaturation is achieved directly rather than by diffusion.Often the batch technique is performed under oil. The oil preventsevaporation and extremely small drops can be used. For this, the term“microbatch” is used. A modification of this technique is not to useparaffin oil (which prevents evaporation completely) but rather usesilicone oil or a mixture of silicone and paraffin oils so that a slowevaporation is possible.

The claimed invention can encompass any and all methods ofcrystallization. One skilled in the art can choose any of such methodsand vary the parameters such that the chosen method results in thedesired crystals.

One preferred method of crystallization of ZAP-70 involves mixing aZAP-70 solution with a “reservoir buffer”, with a lower concentration ofthe precipitating agent necessary for crystal formation. For crystalformation, the concentration of the precipitating agent has to beincreased, e.g. by addition of precipitating agent, for example bytitration, or by allowing the concentration of precipitating agent tobalance by diffusion between the crystallization buffer and a reservoirbuffer. Under suitable conditions such diffusion of precipitating agentoccurs along the gradient of precipitating agent, e.g. from thereservoir buffer having a higher concentration of precipitating agentinto the crystallization buffer having a lower concentration ofprecipitating agent. Diffusion may be achieved e.g. by vapour diffusiontechniques allowing diffusion of water in the common gas phase. Knowntechniques are e.g. vapour diffusion methods, such as the “hanging drop”or the “sitting drop” method. In the vapour diffusion method a drop ofcrystallization buffer containing the protein is hanging above orsitting beside a much larger pool of reservoir buffer. Alternatively,the balancing of the precipitating agent can be achieved through asemipermeable membrane that separates the crystallization buffer fromthe reservoir buffer and prevents dilution of the protein into thereservoir buffer.

Formation of ZAP-70 kinase catalytic domain crystals can be achievedunder various conditions which are essentially determined by thefollowing parameters: pH, presence of salts and additives, precipitatingagent, protein concentration and temperature. The pH may range, forexample, from about 4.0 to 9.0.

The present invention also relates to a computer readable medium havingstored a model of the ZAP-70 catalytic domain crystal structure. In apreferred embodiment, said model is built from all or part of the X-raydiffraction data shown in the atomic coordinates of Table 1.

The present invention provides the structure coordinates of human ZAP-70catalytic domain. The term “structure coordinates” or “atomiccoordinates” refers to mathematical coordinates derived from themathematical equations related to the pattern obtained on diffraction ofa monochromatic beam of X-rays by the atoms (scattering centers) of acrystal comprising a ZAP-70 catalytic domain. The diffraction data areused to calculate an electron density map of the repeating unit of thecrystal. The electron density maps are used to establish the positionsof the individual atoms within the unit cell of the crystal.

Structural coordinates of a crystalline composition of this inventionmay be stored in a machine-readable form on a machine-readable storagemedium, e.g. a computer hard drive, diskette, DAT tape, etc., fordisplay as a three-dimensional shape or for other uses involvingcomputer-assisted manipulation of, or computation based on, thestructural coordinates or the three-dimensional structures they define.For example, data defining the three dimensional structure of a proteinof the ZAP family, or portions or structurally similar homologues ofsuch proteins, may be stored in a machine-readable storage medium, andmay be displayed as a graphical three-dimensional representation of theprotein structure, typically using a computer capable of reading thedata from said storage medium and programmed with instructions forcreating the representation from such data.

In one embodiment of the invention, a method is provided for determiningthe three-dimensional structure of the catalytic domain of ZAP-70comprising:

(i) crystallization of ZAP-70 kinase comprising the catalytic domain ofZAP-70 (SEQ ID No.2), fragment or homologue thereof

(ii) collecting x-ray diffraction data in the form of atomic coordinatesfor said crystal

(iii) utilizing the atomic coordinates of Table 1 in whole or in part todetermine the three-dimensional structure of the catalytic domain ofZAP-70, fragment, or homologue thereof.

In another embodiment of the invention, a method is provided fordetermining the three-dimensional structure of a complex comprising thecatalytic domain of ZAP-70 kinase (SEQ ID No.2), fragment or homologuethereof bound to at least one ligand comprising:

(i) obtaining x-ray diffraction data for a crystal of the complex

(ii) utilizing the atomic coordinates of Table 1 in whole or in part todetermine the three-dimensional structure of the complex.

According to the present invention, a three-dimensional ZAP-70 model isobtainable from a ZAP-70 crystal comprising the catalytic domain ofZAP-70, fragment or homologue thereof. Such a model can be built orrefined from all or part of the ZAP-70 kinase structure data of thepresent invention using the x-ray diffraction coordinates, particularlythe atomic structure coordinates of Table 1.

The knowledge obtained from the three-dimensional model of the catalyticbinding site of ZAP-70 can be used in various ways. For example, it canbe used to identify chemical entities, for example, small organic andbioorganic molecules such as peptidomimetics and synthetic organicmolecules that bind to ZAP-70 and preferably block or prevent a ZAP-70mediated or associated process or event, or that act as ZAP-70 agonists.Using the three-dimensional structure of the ZAP-70 catalytic domain,the skilled artisan constructs a model of the ZAP-70. For example, everyatom can be depicted as a sphere of the appropriate van der Waalsradius, and a detailed surface map of the ZAP-70 catalytic domain can beconstructed.

Chemical entities that have a surface that mimics the accessible surfaceof the catalytic binding site of ZAP-70 can be constructed by thoseskilled in the art. By way of example, the skilled artisan can screenthree-dimensional structural databases of compounds to identify thosecompounds that position appropriate functional groups in similar threedimensional structural arrangement, then build combinatorial chemistrylibraries around such chemical entities to identify those with highaffinity to the catalytic binding site of ZAP-70.

In one embodiment of the invention, a method is provided for identifyinga ligand or low molecular weight compound that binds to the catalyticdomain of ZAP-70 kinase comprising the steps of:

(i) using the three-dimensional structure of the catalytic domainderived in whole or in part from the set of atomic coordinates in Table1 to select a potential ligand or low molecular weigh compound thatbinds to the catalytic domain of ZAP-70

(ii) selecting those ligands or low molecular weight compounds that bindto the catalytic domain of ZAP-70.

In another embodiment of the invention, a method is provided foridentifying a ligand or low molecular weight compound that binds to thecatalytic domain of ZAP-70 kinase wherein the catalytic domain of ZAP-70comprises at least the ATP binding site of said domain,

In yet another embodiment of the invention, a method is provided foridentifying ligands which inhibit the biological activity of ZAP-70kinase.

Ligands or small molecular compounds can be identified from screeningcompound databases or libraries and using a computational means to forma fitting operation to a binding site on the catalytic domain of ZAP-70kinase. The three dimensional structure of the catalytic domain ofZAP-70 as provided in the present invention in whole or in part by thestructural coordinates of Table 1, can be used together with variousdocking programs.

The potential inhibitory or binding effect of a chemical entity onZAP-70 may be analyzed prior to its actual synthesis and testing by theuse of computer-modeling techniques. If the theoretical structure of thegiven chemical entity suggests insufficient interaction and associationbetween it and ZAP-70, the need for synthesis and testing of thechemical entity is obviated. However, if computer modeling indicates astrong interaction, the molecule may then be synthesized and tested forits ability to bind to ZAP-70. Thus, expensive and time-consumingsynthesis of inoperative compounds may be avoided.

An inhibitory or other binding compound of ZAP-70 may be computationallyevaluated and designed by means of a series of steps in which chemicalentities or fragments are screened and selected for their ability toassociate with the individual binding sites of ZAP-70. Thus, one skilledin the art may use one of several methods to screen chemical entities orfragments for their ability to associate with ZAP-70. This process maybegin by visual inspection of, for example, the binding site on acomputer screen based on the structural coordinates of Table 1 in wholeor in part. Selected fragments or chemical entities may then bepositioned in a variety of orientations, or “docked,” within thecatalytic binding site of ZAP-70. Docking may be accomplished usingsoftware such as Quanta and SyLyl, followed by energy minimization andmolecular dynamics with standard molecular mechanics force fields, suchas CHARMM and AMBER. Specialized computer programs may be of use forselecting interesting fragments or chemical entities. These programsinclude, for example, GRID, available from Oxford University, Oxford,UK; 5 MCSS or CATALYST, available from Molecular Simulations,Burlington, Mass.; AUTODOCK, available from Scripps Research Institute,La Jolla, Calif.; DOCK, available from University of California, SanFrancisco, Calif., and XSITE, available from University College ofLondon, UK.

Using molecular replacement to exploit a set of coordinates such asthose of Table 1 of the invention, the structure of a crystallineZAP-kinase catalytic domain or portion thereof can for example, be boundto one or more ligands or low molecular weight compounds to form acomplex.

The term “molecular replacement” refers to a method that involvesgenerating a preliminary structural model of a crystal whose structuralcoordinates are unknown, by orienting and positioning a molecule whosestructural coordinates are known, e.g., the ZAP-70 kinase catalyticdomain coordinates within the unit cell of the unknown crystal, so as tobest account for the observed diffraction pattern of the unknowncrystal. Phases can then be calculated from this model, and combinedwith the observed amplitudes to give an approximated Fourier synthesisof the structure whose coordinates are unknown. This in turn can besubject to any of the several forms of refinement to provide a finalaccurate structure of the unknown crystal. Using the structuralcoordinates provided by this invention, molecular replacement may beused to determine the structural coordinates of a crystalline cocomplex, unknown ligand, mutant, or homolog, or of a differentcrystalline form of ZAP-70 kinase. Additionally, the claimed crystal andits coordinates may be used to determine the structural coordinates of achemical entity that associates with ZAP-70.

“Homology modeling” according to the invention involves constructing amodel of an unknown structure using structural coordinates of one ormore related proteins, protein domains and/or one subdomains such as thecatalytic domain of ZAP-70 kinase. Homology modeling may be conducted byfitting common or homologous portions of the protein or peptide whosethree dimensional structure is to be solved to the three dimensionalstructure of homologous structural elements. Homology modeling caninclude rebuilding part or all of a three dimensional structure withreplace of amino acids or other components by those of the relatedstructure to be solved.

Molecular replacement according to the present invention, uses amolecule having a known structure. The three-dimensional structure ofthe catalytic domain of ZAP-70 provided in whole or in part in Table 1in a machine-readable form on a data-carrier can be used as a startingpoint to model the structure of an unknown crystalline sample. Thistechnique is based on the principle that two molecules which havesimilar structures, orientations and positions in the unit cell diffractsimilarly. Molecular replacement involves positioning the knownstructure in the unit cell in the same location and orientation as theunknown structure. Once positioned, the atoms of the known structure inthe unit cell are used to calculate the structure factors that wouldresult from a hypothetical diffraction experiment. This involvesrotating the known structure in the six dimensions (three angular andthree spatial dimensions) until alignment of the known structure withthe experimental data is achieved. This approximate structure can befine-tuned to yield a more accurate and often higher resolutionstructure using various refinement techniques. For instance, theresultant model for the structure defined by the experimental data maybe subjected to rigid body refinement in which the model is subjected tolimited additional rotation in the six dimensions yielding positioningshifts of under about 5%. The refined model may then be further refinedusing other known refinement methods. The present invention also enableshomologues and mutants of ZAP-70 catalytic domain and the solving oftheir crystal structure. Based on the three-dimensional structure ofZAP-70 catalytic domain as provided in the present invention and usingthe atomic coordinates of Table 1 in whole or in part, the effects ofsite-specific mutations can be predicted. More specifically, thestructural information provided herein permits the identification ofdesirable sites for amino acid modification, particularly amino acidmutation resulting in substitutional, insertional or deletionalvariants. Such variants may be designed to have special properties,particularly properties distinct from wild-type ZAP-70 catalytic domain,such as altered catalytic activity. Substitutions, deletions andinsertions may be combined to arrive at a desired variant. Such variantscan be prepared by methods well-known in the art, e.g. starting fromwild-type ZAP-70 catalytic domain, or by de novo synthesis.).

ZAP-70 catalytic domain may also crystallize in a form different fromthe one disclosed herein. The structural information provided, forexample, in SEQ ID No. 2 and Table 1 in whole or in part, is also usefulfor solving the structure of other crystal forms. Furthermore, it mayserve to solve the structure of a ZAP-70 catalytic domain mutant, aZAP-70 catalytic domain co-complex or a sufficiently homologous protein.

The ZAP-70 catalytic domain structural information provided herein isuseful for the design of ligands or small molecule compounds which arecapable of selectively interacting with ZAP-70 catalytic domain andthereby specifically modulating the biological activity of ZAP-70.Furthermore, this information can be used to design and prepare ZAP-70mutants, e.g. mutants with altered catalytic activity, model thethree-dimensional structure and solve the crystal structure of proteins,such as ZAP-70 catalytic domain homologues, ZAP-70 catalytic domainmutants or ZAP-70 catalytic domain co-complexes, involving e.g.molecular replacement.

The present invention provides a method for designing a ligand or lowmolecular weight compound capable of binding with ZAP-70 catalyticdomain, said method comprising:

(i) using the atomic coordinates of Table 1 in whole or in part todetermine the three-dimensional structure of the ZAP-70 catalytic domain

(ii) probing said three-dimensional structural of the ZAP-70 catalyticdomain with candidate ligands or low molecular weight compounds todetermine which bind to the catalytic domain of ZAP-70

(iii) selecting those ligands or low molecular weight compounds whichbind to the catalytic domain of ZAP-70

(iv) optionally, modifying those ligands or low molecular weightcompounds which bind to maximize physical binding properties such assolubility, affinity, specificity or potency.

Preferred is a method for designing a ZAP-70 inhibitor which interactsat the catalytic binding site. The present invention also relates to thechemical entity or ligand identified by such method. One approachenabled by this invention is the use of the structural coordinates ofZAP-70 catalytic domain to design chemical entities that bind to orassociate with ZAP-70 kinase and alter the physical properties of thechemical entities in different ways. Thus, properties such as, forexample, solubility, affinity, specificity, potency, on/off rates, orother binding characteristics may all be altered and/or maximized. Onemay design desired chemical entities by probing an ZAP-70 crystalcomprising the catalytic domain with a library of different entities todetermine optimal sites for interaction between candidate chemicalentities and ZAP-70. For example, high-resolution x-ray diffraction datacollected from crystals saturated with solvent allows the determinationof where each type of solvent molecule adheres. Small molecules thatbind tightly to those sites can then be designed and synthesized andtested for the desired activity. Once the desired activity is obtained,the molecules can be further altered to maximize desirable properties.

The invention also contemplates computational screening ofsmall-molecule databases or designing of chemical entities that can bindin whole or in part to ZAP-70 catalytic domain. They may also be used tosolve the crystal structure of mutants, co-complexes, or the crystallineform of any other molecule homologous to, or capable of associatingwith, at least a portion of ZAP-kinase. One method that may be employedfor this purpose is molecular replacement. An unknown crystal structure,which may be any unknown structure, such as, for example, anothercrystal form of ZAP-70 kinase catalytic domain, an ZAP-70 kinasecatalytic domain mutant or peptide, or a co-complex with ZAP-70 kinase,or any other unknown crystal of a chemical entity that associates withZAP-70 that is of interest, may be determined using the whole of part ofthe structural coordinates set forth in Table 1. This method provides anaccurate structural form for the unknown crystal far more quickly andefficiently than attempting to determine such information without theinvention herein.

In one preferred embodiment of the invention, candidate ligands arescreened in silico. The information obtained can thus be used to obtainmaximally effective inhibitors or agonists of ZAP-70. The design ofchemical entities that inhibit or agonize ZAP-70 generally involvesconsideration of at least two factors. First, the chemical entity mustbe capable of physically or structurally associating with ZAP-70,preferably at the catalytic site of ZAP-70. The association may be anyphysical, structural, or chemical association, such as, for example,covalent or noncovalent bonding, or van der Waals, hydrophobic, orelectrostatic interactions. Second, the chemical entity must be able toassume a conformation that allows it to associate with ZAP-70,preferentially at the catalytic site of ZAP-70. Although not allportions of the chemical entity will necessarily participate in theassociation with ZAP-70, those non-participating portions may stillinfluence the overall conformation of the molecule. This in turn mayhave a significant impact on the desirability of the chemical entity.Such confirmational requirements include the overall three-dimensionalstructure and orientation of the chemical entity in relation to all or aportion of the binding site.

Once a compound has been designed or selected by the above methods, theefficiency with which that compound may bind to ZAP-70 may be tested andmodified for the maximum desired characteristic(s) using computationalor experimental evaluation. Various parameters can be maximizeddepending on the desired result. These include, but are not limited to,specificity, affinity, on/off rates, hydrophobicity, solubility, andother characteristics readily identifiable by the skilled artisan.

The present invention also relates to identification of compounds whichmodulate ZAP-70. Preferred are compounds which inhibit ZAP-70 activityand are potentially useful for the treatment of diseases and conditionssuch as those which involve T cell and lymphocyte activation.

The present invention enables the use of molecular design techniques,particularly the rational drug design approach, to prepare new orimproved chemical entities and compounds, including ZAP-70 inhibitors,capable of irreversibly or reversibly, modulating ZAP-70 activity.Improved entities or compounds means that these entities or compoundsare superior to the “original” or parent compound they are derived fromwith regard to a property relevant to therapeutic use includingsuitability for in vivo administration, e.g. cellular uptake,solubility, stability against (enzymatic) degradation, binding affinityor specificity, and the like. For example, on the basis on theinformation provided herein it is possible to specially design ZAP-70inhibitors which covalently, or preferably non-covalently, bind toZAP-70. Such inhibitors may act in a competitive or uncompetitivemanner, bind at or close to the active site of ZAP-70 or actallosterically.

In the design of ZAP-70 modulators the following aspects should beconsidered: (i) if the candidate compound is capable of physically andstructurally associating with ZAP-70 kinase catalytic domain, and/or(ii) if the compound is capable of assuming a conformation allowing itto associate with ZAP-kinase catalytic domain. Advantageously, computermodelling techniques are used in the process of assessing theseabilities for the modulator as a whole, or a fragment thereof—in orderto minimize efforts in the synthesis or testing of insuccessfulcandidate compounds. Specialized computer software is well-known in theart.

Another design approach is to probe a ZAP-70 catalytic domain crystalwith a variety of different chemical entities to determine optimal sitesfor interaction beween candidate ZAP-70 inhibitors and the targetenzyme. Yet another possibility which arises from the present inventionis to screen computationally small molecule data bases for chemicalentities or compounds that are capable of binding, in whole or in part,to ZAP-70 catalytic domain. The quality of fit to the binding site maybe judged e.g. by shape complementarity or by estimated interactionenergy. Knowledge of the three-dimensional arrangement of themodifications can be then utilized for the design of new ZAP-70 ligandsor low molecular weight compounds such as selective inhibitors.

Chemical entities that are capable of associating with the ZAP familymember may inhibit its interaction with naturally occurring ligands ofthe protein and may inhibit biological functions mediated by suchinteraction. In the case of ZAP-70, such biological functions includeactivation of T cells during an immune response. Such chemical entitiesare potential drug candidates.

Compounds of the structures selected or designed by any of the foregoingmeans may be tested for their ability to bind to a ZAP family protein,inhibit the binding of a ZAP family protein to a natural or non-naturalligand therefor, and/or inhibit a biological function mediated by a ZAPfamily member.

The following examples serve to illustrate the present invention butshould not be construed as a limitation thereof. The inventionparticularly relates to the specific embodiments described in theseexamples. Compounds first identified by any of the methods describedherein are also encompassed by this invention.

EXAMPLES Example 1 Initial Purification of Full-Length ZAP Kinase

The full length amino acid sequence of the ZAP-70 kinase is given in SEQID No. 1. N-terminally His₆-tagged full-length ZAP kinase is expressedin Sf9 cells, this differs from the wild-type sequence in that theN-terminal is modified by insertion of a hexa-histidine sequence inbetween the N-terminal methionine and proline (position 2), such thatthis proline is now in position 8. Cell pellets are harvested and frozenat −80° C. until required. A 39 g wet cell pellet is suspended in 350 mlice-cold buffer A (50 mM sodium phosphate pH 8, containing 12 EDTA-freeComplete™ protease inhibitor tablets, 10 mM β-mercaptoethanol, 10% v/vglycerol, 0.1 mM MnCl₂, 10 mM imidazole and 300 mM NaCl). The cells arelysed for 3 minutes on ice using a Heidolph-Diax tissue-grinder followedby 10 strokes in a glass-teflon homogeniser. The resultant lysate iscentrifuged for 45 min at 43,000 g at 4° C. and subsequently filteredthrough successive glass-fibre, 1.2 μM and 0.43 μM filter membranes.This clarified supernatant is loaded at a flow-rate of 2 ml/min onto anXK16/20 chromatography column (Amersham Biosciences) containing 20 mlNi—NTA-agarose (Qiagen) affinity resin equilibrated with buffer A. Onceall the material has been loaded, the column is washed (at a flow-rateof 4 ml/min) with buffer A until the UV-absorbance of the flow-throughmaterial has once again returned to baseline levels. At this point(using the same flow-rate), buffer B (25 mM Tris-HCl pH8, 10% v/vglycerol, 50 mM NaCl and 250 mM imidazole) is applied to the column andthe peak of protein which elutes is collected. This material is loadeddirectly onto a 16 ml column of γ-aminophenyl-ATP sepharose equilibratedwith buffer C (25 mM Tris pH 8.0 containing: 30% v/v glycerol, 1 mM DTT,1 mM MgCl₂ and 50 mM NaCl) at a flow-rate of 2 ml/min. The column iseluted by applying a gradient of 0-1M NaCl in buffer C over 7 columnvolumes. The eluted peak is concentrated by ultrafiltration using a30,000 M_(r) cut-off membrane (Amicon) to approximately 7 ml and furtherpurified using a Superdex 75 (XK16/60) size-exclusion columnequilibrated with buffer C (but without 50 mM NaCl). The fractionscontaining ZAP 70 monomer are collected and pooled prior toconcentration to 2.5 mg/ml and subsequent limited proteolytic digestion.

Full-length ZAP-70 is eluted from the NTA-agarose column at a purity ofapproximately 60% as determined by reducing SDS-PAGE. Subsequentchromatography on a 16 ml column of γ-aminophenyl-ATP sepharose gives arather broad peak of much higher purity which can be concentrated.Detailed analysis of this peak reveals that the earlier elutingfractions contain predominantly aggregated material and that a discretepeak towards the end of the profile contains most of the monomeric ZAPof high purity. Size-exclusion chromatography gives a major peakcomprising ˜90% of the protein, the remainder eluting slightly earlierin a position where dimeric or aggregated protein would be expected toelute. At this stage the purity of the preparation is in excess of 90%and suitable for use in the limited proteolytic definition of minimalkinase domains. At this stage, highest purity is very important so as tominimise the number of additional sequences present followingproteolytic digestion.

Example 2 Proteolytic Catalytic Domain Definition

ZAP-70 is incubated for 20 h at room temperature at a 1:100concentration ratio with the following proteases: thermolysin,carboxypeptidase A, thrombin, Arg C, Glu C, Factor Xa, CarboxypeptidaseY, chymotrpsin, Lys C, Asp N, elastase, trypsin and subtilisin (1:1ratio). Following incubation samples are removed, subjected to reducingSDS-PAGE electrophoresis (Novex 4-20% gels, Invitrogen) and comparedwith non-digested controls. In the cases where faster migrating bandsare observed, which are of sufficient size (˜30 kDa) to contain thecatalytic domain, samples are re-run on SDS-PAGE and Western-blottedusing an anti-His₆ antibody (Sigma, H-1029). This is in order toidentify N-terminal and C-terminal ZAP-70 fragments (the His₆-tag is atthe N-terminus, consequently forms showing anti-His₆ immunoreactivityare truncated at the C-terminus and are of no interest).Non-immunoreactive fragments are subjected to SDS-PAGE and transferredelectrophoretically to PVDF membranes, the bands visualised, excised andtheir N-terminal sequences analysed.

Following digestion with thermolysin, trypsin, Glu C, Asp N andelastase, faster migrating bands are observed which are of sufficientsize (˜30 kDa) to contain the catalytic domain. When Western-blottedagainst the (His)₆ N-terminal tag, non-immunoreactive fragments areproduced by trypsin, elastase and thermolysin digestion, and are therebydefined as being C-terminal in origin. These fragments are sequenced.Trypsin and Thermolysin digestion both give a fragment with Isoleucine299 as N-terminus. Elastase produces an arginine298 fragment andthermolysin an additional leucine277 fragment. Based upon these results,ZAP catalytic domains beginning with leucine277 and arginine298 areidentified as being potentially suitable for crystallisation.

Example 3 Cloning of PreScission™ I and II Constructs

Previous attempts to purify a number of catalytic domain constructsproved difficult due to low levels of expression of soluble protein andinstability of these proteins. This instability might be, in part, dueto incorrect in-vivo folding of the isolated domains and in part due tonon-optimal construct length. Therefore, the full-length ZAP-70 isexpressed, flanked by the PreScission™ protease recognition sequences tofacilitate efficient proteolytic release of the desired domain. Based onthe results obtained from the limited proteolysis of the full-lengthversion of ZAP-70, two constructs were made: PreScission™I, aC-terminally His₆-tagged ZAP-70 with a PreScission site insertedimmediately prior to leucine 277 (residue 285 in construct) andPreScission II™, which contained two such sites, one upstream ofarginine298 (residue 306 in construct) and one upstream of theC-terminal His₆ tag, so that this could be removed simultaneously. Withthe oligonucleotide MG474 and RS366 (see: SEQ ID No.3 and 4respectively) and the plasmid NPL2173 encoding the wild type full-lengthZAP-70 gene (Genbank Accession Nr. L05148), a DNA fragment is amplifiedwhich upon integration into the original NPL2173 allows the introductionof the PreScission™ cleavage site between alanine297 and arginine298.Another cleavage site is added after alanine619, preceeding the(His)₆-tag. The integration of the PCR fragment is done as describedearlier (Geiser et al. Biotechnology 2001). The resulting plasmid issequenced and the correct clone called pXI347 (PlasNova NPL003792).Similarly the plasmid pXI345 (NPL003793) is constructed by integratingthe PCR fragment obtained from the NPL2173 plasmid template with theoligonucleotides MG475 and MG479 (SEQ ID No 5 and SEQ ID No 6) InpXI345, the PreScission™ cleavage site is integrated betweenthreonine282 and leucine277 and the PreScission™ cleavage site in frontof the (His)₆ tag is removed. The two plasmids are then introduced bytransfection together with a linearized baculovirus DNA into insectcells. The numbering of amino acids is based on the sequences differsfrom that of Genbank Accession number L05148, by virtue of the inclusionof the purification tag and the inserted protease recognition sequences.

Based on the results of the limited proteolysis of the full sized ZAP-70introduced after positions 276, 297 and after amino acid position 619,PreScission™ cleavage sites. The plasmids encoding the new mutants ofZAP-70 are called pXI345 and pXI347 respectively. These plasmids encodethe protein ZAP PreScission™ I and ZAP PreScission™ II respectively. Asa result of the mutations, complete and highly specific proteolysis ofthe full-length proteins can be carried out with a high quantitativerecovery of the catalytic domain of ZAP-70.

Example 4 Expression and medium-scale fermentation of PreScission II ZAPin Baculovirus

Sf21 cells propagated in Excell 401 medium with 10% fetal calf serum aretransfected with 500 ng of each recombinant transfer vector and 5 μl oflinear AcNPV virus DNA (BacPAK 6) by lipofection using Bacfectin astransfection reagent (both BD/Clontech, Palo Alto, Calif.). After fivedays of incubation, the transfection supernatants are harvested andsubjected to plaque assay, to derive a homogenous viral population. Theisolated virus plaque picks are further amplified by infection of Sf21cells grown in suspension in Excell 401 plus 1% FCS in roller culture,until full working virus stocks of both viruses are developed. These areagain titered by plaque assays.

Large scale productions are carried out using the Wave bioreactor (WaveBiotech AG, Tagelswangen, Switzerland) at 10 I working volume. Sf9 cellsgrowing in SF900 II medium (Gibco/Life Technologies) are inoculated inthe Wave bag and allowed to grow for three consecutive days, reachingmaximal cell densities of approx. 5×10⁶ cells ml. During the cultivationand infection process the airflow, the rocking rate and the rockingangle of the Wave reactor thermoplate are monitored and adjusted. TheSf9 cells are infected at cell densities of 1.6-4.9×10⁶ cells/ml anddifferent multiplicities of infection (m.o.i.) between 0.5, 1 and 2m.o.i. Simultaneously with virus addition, yeastolate (Gibco/LifeTechnologies) is fed to the cultures at a final concentration of 4 g/l.Cell density as well as cell viability is carefully recorded during theinfection period.

Plaque assays of the amplified working virus stocks give rise to titersof 5.6×10⁷ pfu/ml for the ZAP70 PreScission™ I construct and 1.7×10⁸pfu/ml for the ZAP-70 PreScission™ II construct. Both are subsequentlyused for 10 litre large-scale production of the two PreScission™ ZAPconstructs. Both proteins are well-expressed and at least partiallysoluble; however, although LC-MS of NTA superflow purified PreScission™II showed several peaks with masses of 72,404, 72,478, 72,557 and 72,635which were thought to correspond to non-, mono-, di- andtri-phosphorylated full-length kinase, the PreScission™ I material gavesuch a heterogeneous LC-MS spectrum that it was impossible to assignmasses, therefore all expression efforts were concentrated towardsproduction of the PreScission™ II construct.

Example 5 Method for Optimising Harvesting of the Sf9 Cultures

The baculovirus expression system is a lytic system; as the infectionproceeds, cells die and lyse, losing their contents into the medium. Inthe case of the expression of proteins such as ZAP, which are expressedintracellularly, there is a small “window” of expression in whichmaximal protein expression occurs before this is lost through celllysis. Typically Western blotting will be used in conjunction with atime course of infection as well as variation of the multiplicity ofinfection (m.o.i.) to determine this time-point. However, in the case ofZAP PreScission™ II, the observation is made that increasing levels ofexpression are also accompanied by increasing levels of insolubleprotein. Therefore, rapid small-scale purifications lysing 1 gquantities of cells give an “on-line” readout of “purifiable” ZAP.

1 g cell pellets are removed at different time points duringfermentation and lysed as described previously (but using 15 ml lysisbuffer, containing 1 Complete™ EDTA-free protease inhibitor tablet). Dueto the scale-down, a 0.5 ml Ni—NTA-agarose column is used and the wholeprocess from lysis through to analytical RP-HPLC estimate of the contentof isolated protein is reduced to 34 hours. With an optimised harvesttime of 48 h, the yield of soluble ZAP can be increased 4-fold toapproximately 0.75 mg purifiable ZAP/g cells or −7.5 mg/litre culture.

Example 6 Staurosporin Binding to the ZAP Kinase Catalytic Domain

ZAP-70 kinase catalytic domain (R₂₉₈-A₆₁₉; SEQ ID No.2) defined bylimited proteolysis is recloned as the full-length ZAP-70 kinase with aC-terminal His₆-affinity tag, but flanked by two PreScission™ proteasesites. Expression is carried out using SF9 cells grown in 10 litre Wave™bioreactors (0.45 m.o.i; 48 h). Cells are lysed in ice-cold buffer A (50mM NaPO₄, 10% v/v glycerol, 10 mM β-mercaptoethanol, 300 mM NaCl, 10 mMImidazole; pH 8.0) containing Complete™ EDTA-free protease inhibitor.The clarified lysate is passed over a 20 ml Ni—NTA-agarose column, thecolumn washed with buffer A and then eluted with buffer B (25 mM Tris,10% v/v glycerol, 50 mM NaCl, 250 mM Imidazole; pH 8.0). Allchromatography steps are either carried out on-ice or using jacketed,cooled columns. The protein is immediately desalted into 25 mM TrispH8.0, containing 1 mM EDTA, 1 mM DTT, 30% v/v glycerol and 150 mM NaCl,(using a 50 ml sephadex G-25 desalting column; HiPrep™ 26/10 AmershamBiosciences) concentrated and staurosporin added to 2-Molar excess (byaddition of the correct volume of staurosporin dissolved in DMSO to 2mg/ml).

The protein solution (60 ml) is frozen at −80° C. until required thenconcentrated using a 30,000 M_(r) cut-off ultrafiltration membrane(Amicon) down to 10-15 ml prior to size-exclusion chromatography usingan XK26/90 column packed with Superdex 75™ and equilibrated with 25 mMTris pH 8, 1 mM EDTA, 1 mM DTT, 150 mM NaCl and 30% v/v glycerol.Fractions are collected, those corresponding to the monomeric material(ca. 40 ml) are pooled and incubated with PreScission™ protease toexcise the catalytic domain from the rest of the molecule. Typically 40ml of solution, containing 42 mg ZAP PreScission™ II is digested for 135min at room temperature with 420 μl PreScission™ protease solution. Thecleavage reaction is monitored by reversed phase HPLC so that thereaction can be stopped as quickly as possible by immediately desaltinginto buffer C (20 mM NaPO₄, 5 mM DTT, 10 mM NaCl, 1 mM MgCl₂: pH 7.2).Typically as 3×14 ml portions, applied at a flow-rate of 5 ml/minute toa HiLoad™ 26/10 column. The desalted protein, containing a mixture ofmonophosphorylated (25%) and non-phosphorylated (75%) ZAP is applied toan HR10/8 cation-exchange column (Mono S™ Amersham Biosciences)equilibrated in buffer C. The column is loaded at a flow-rate of 1ml/minute and eluted at two ml/min using a 0-250 mM NaCl gradient over512 ml.

Two major peaks are eluted, the monophosphorylated protein eluting atapproximately 80 mM NaCl, the non-phosphorylated protein, slightly laterat approximately 100 mM NaCl. The non- and mono-phosphorylated ZAPkinase catalytic domain peaks are collected separately, desalted (HiLoad26/10 column) into 20 mM HEPES pH 7.2 (containing 5 mM DTT, 1 mM MgCl₂,150 mM NaCl and 1% v/v ethyleneglycol). Staurosporine is again added to10 Molar excess to both forms which are subsequently concentrated to1040 mg/ml for crystallisation. This desalting step is critical, becauseit removes the glycerol required for chromatography (without which, theprotein precipitates) and replaces it with a low concentration ofethylene glycol which sufficiently stabilises the protein through theconcentration step, but doesn't interfere with the subsequentcrystallization. 30% V/v glycerol, on the other hand, is not suitablefor crystallisation as it has too large an influence on the evaporativesitting-drop process. In the case of the non-phosphorylated protein,half of the eluted peak, 36 ml is concentrated to 130 μl and a finalconcentration of 36 mg/ml.

By optimisation of the fermentation and harvest conditions, the level ofZAP expression is increased such that the purity of ZAP PreScission™ IIbeing eluted from the NTA column is in excess of 75% and could beadequately purified by an additional size-exclusion chromatography stepprior to cleavage. Following cleavage with PreScission™ protease, twobands are observed of similar mass representing the kinase andN-terminal portions of the molecule. Cation-exchange chromatography isapplied to separate the two forms. The N-terminal portion passed throughthe column under the conditions used. The two peaks that are eluted fromthe column represented two different phosphorylated forms; themonophosphorylated protein eluting at approximately 80 mM NaCl and thenon-phosphorylated protein, slightly later at approximately 100 mM NaCl.These different forms are collected separately for crystallisation. Theyield of the mono-phosphorylated form is approximately 4-fold lower thanthe non-phosphorylated form, therefore most crystallography effortsconcentrated on the non-phosphorylated form.

Example 7 Crystallisation of PreScission II ZAP

9 mg/ml ZAP-70 non-phosphorylated catalytic kinase domain in 20 mMHepes, 5 mM DTT, 1 mM MgCl₂, 150 mM NaCl, 30% Glycerol, andstaurosporine, are used for initial crystallization screening using 96well sitting drop crystallography plates. The first promisingmicrocrystals are obtained with crystallization screen at 10° C.Optimization of these crystallisation conditions is carried out byhanging drop vapor diffusion. The crystallisation screen at 10° C. hasthe following crystallisation conditions: 0.1 M Tris pH 7.5, 0.1 M KCl,18% PEG 5000 monomethylether. Optimisation of this crystallisationcondition along with optimisation of the formulation of the proteinpreparation results in larger crystals. Hanging drop vapor diffusion isused for optimisation. Diffracting single crystals are obtained with 29mg/ml Zap70 nonphosphorylated kinase domain in 20 mM Hepes, 5 mM DTT, 1mM MgCl₂, 150 mM NaCl, 1% Ethylene glycol, and staurosporine. Theoptimal growth condition is: 0.1 M Tris HCl pH 7.5, 0.2 M KCl, 20% PEG5000 monomethylether at a crystallisation temperature of 10° C. Crystalsappear after 1-2 days and optimal crystal size is reached after 1-2weeks. Some single crystals grow, but most single fragments are obtainedby breaking apart clusters.

Example 8 Protein Production and Crystallization of the Human ZAP-70Protein Kinase Catalytic Domain

SEQ ID No.2 of the human ZAP-70 protein kinase catalytic domain(non-phosphorylated) is used for crystallization The construct comprisesZAP-70 residues 298 to 619 plus two additional residues from thePreScission™ cleavage site at the N-terminus and 6 residues from thePreScission™ cleavage site at the C-terminus. Small, butwell-diffracting single crystals are obtained with a preparation of 29mg/ml protein concentration and 1% Ethylene glycol. Optimal growthconditions are 20% PEG 5000 monomethylether, 0.1 M Tris HCl pH 7.5, 200mM KCl. Crystals appear after 1-2 days and optimal crystal size isreached after 1-2 weeks. Some single crystals form but most singlefragments are obtained by breaking apart clusters.

Cryo-Protection

Crystals are transferred from the drop into a solution consisting of thecrystallization solution (well solution) plus 20% (v/v) of glycerol and1 mM inhibitor. Crystals mounted in a 0.05 μm cryo loop are soaked inthis cryo buffer for about 10-15 sec and then dipped into liquidpropane.

Data Collection

A crystal is frozen in liquid propane and diffraction data are collectedat 80K with a MAR CCD camera at the SLS in Villingen, Switzerland. Awavelength of 0.9803 A is used. 340 images are collected with 1.0°oscillation each, using an exposure time of 6 sec per frame and acrystal-to-detector distance of 140 mm. Raw diffraction data areprocessed and scaled with the HKL program suite version 1.96.6(Otwinowski and Minor, 1996). Crystal data and data statistics are shownin Table 2.

Structure Determination and Refinement

The structure of the catalytic Zap70 kinase domain is determined bymolecular replacement, using the coordinates of the LCK kinase domainx-ray structure (pdb: 3LCK, Yamaguchi and Hendrickson, 1996) as searchmodel. Residues 245 to 501 of LCK are used and the phospho-Tyr residue394 is removed for sequence similarity comparisons.

Molecular replacement is performed with the auto molecular replacementscript in CCP4, using data to a maximal resolution of 4.0 Å. A 80%fraction completeness of the model with 50% fraction similarity to theinput structure and 2 molecules in the asymmetric unit is expected. Aclear solution is found and after an initial refinement in CNX using thestandard script refine.inp the structure has an R-factor of 41.7%(R-free 43.5%). Inspection of the σ_(A)-weighted Fo-Fc electron densitymap with the program 0 version 7.0 (Jones et al., 1991) reveals a strongdensity for most of the C-alpha trace and most of the side chains. Thereare several insertions and deletions and a number of loops which arefound outside the electron density and have to be corrected manually.

The model of the human ZAP-70 protein kinase catalytic domain is builtand adjusted to fit the density where necessary. Insertions, mutationsand deletions are made accordingly. The numbering was changed using thenumbering of the SwissProt Accession number P43403 entry for ZAP-70. Thestructure is refined by a number of cycles of torsion angle dynamics andenergy minimization, interspersed by model rebuilding steps. Forrefinement, the “refine.inp” script of CNX 2000 is used, with thefollowing (non-default) option: Bulk solvent correction (based on themask method).

Cross-validation is used throughout refinement using a test setcomprising 5% of the reflections. Water molecules are identified withthe CNX script water_pick.inp, and selected based on difference peakheight (greater than 3.0σ), hydrogen-bonding and distance criteria. NCSrestrain is used for the two molecules in the asymmetric unit.

The quality of the final refined model is assessed with the programs CNX2000 (Brünger, 1998) (see: FIG. 7). Pictures are made in O (Jones etal., 1991) or WebLab ViewerLite 3.5 (Molecular Simulations, Inc.).

Results

Small single crystals of the human Zap70 kinase domain are obtained withPEGMME at pH 7.5. The crystals grow in space group P1 with 2 monomersper asymmetric unit. The structure is determined by molecularreplacement. The final model includes two kinase domains (residue 331 to603), one molecule of staurosporine per kinase domain and 261 watermolecules. It has a good geometry with a rms deviation of 0.011 Å onbond lengths and 1.3° on bond angles. The final R-factor was 0.182(Rfree=0.209) for all reflections between 19.26 Å and 1.90 Å.

Overall Structure

The crystal structure is extremely well defined, the full c-alpha tracebetween residue 331 and 603 is defined. All loops and important residueshave good electron density. The B-factor distribution is as expected.The staurosporine-binding site and all interactions with the kinasedomain can be described in detail. The quality of the model is good, thefinal R-factor is 18.2% (R-free 20.9%).

The ZAP-70 kinase domain folds into the typical kinase domain fold. Mostof the residues are well defined by the electron density with a fewexceptions: The N-terminal residues 296 to 330 and the C-terminalresidues 604 to 625 are completely disordered and therefore not visiblein the x-ray structure. There are a few side chains at the surface ofthe molecules that do not show a well-defined electron density. A numberof side chains clearly show alternating side chain positions. Those werenot refined; there is only one side chain with alternating conformationclose to the staurosporin-binding site, which could be of importance:SER 478.

There is an electron density of the linker region between β5 and αD.This region has an unusual sequence (Ala417-Gly418-Gly419-Gly420-Pro421)and forms part of the staurosporine binding site. This region is wellordered and the electron density is well defined. The two importantcontacts (Glu 415O-N1, Ala 417N -O5).

Staurosporine-Binding Site

The binding site for staurosporine in mostly shaped by the hydrophobicside chains of the following residues: Leu344, Phe349, Val352, Val399,Met414, Met416, Ala417, Leu468. Deep in the binding pocket, two polarinteractions contribute to the staurosporine binding: the main chaincarbonyl oxygen of residue Glu415 binds to nitrogen N1 of staurosporineand the main chain peptide nitrogen of residue Ala417 interacts with thecarbonyl oxygen 05 of staurosporine. At the other end of thestaurosporine molecule there are a few polar interactions between thesugar moiety and the protein. The staurosporine methoxy group forms onlyvan der Waals contacts, but the -N-Met group interacts with the proteinthrough a hydrogen bridge network that is formed by a number of solventmolecules and the side chains of residue Lys424, His423, Arg465 (alsoinvolving the carboxyl oxygen of the peptide bond), Asp479, Asn466.

An alignment (ClustalW) with some of the well-known kinase structuresshow that the sequence variability is rather high. Nevertheless, if thec-alpha traces get superimposed, usually a relatively good fit isnoticed (53-59%).

From the alignment, many kinases have insertions or deletions comparedto Zap70 which makes is extremely difficult to model the structure inevery detail. Nevertheless, the ATP-binding site has a relativelyconserved structure and is easier to model than most of the rest of thekinase domain.

Phosphorylation Sites

Phosphorylation of residues in the activation segment causesconformational changes in the catalytic kinase domain that lead to thecorrect positioning of substrate binding residues and catalyticresidues, and relief of steric blocking to enable access of substrate tothe catalytic site.

The kinase domain crystallized here, is not phosphorylated. However,Zap70 contains a number of tyrosine residues, which can bephosphorylated in vivo and contribute to the regulation of the kinaseactivity and adaptor molecule binding. Due to the fact, that we aretargeting the ATP binding site, it should not be a huge drawback that weonly have the structure of the non-activated/phosphorylated kinasedomain.

The phosphorylation sites 474, 492, 493, 597, and 598 are defined in thex-ray structure. Tyrosine 492 and 493 are both located in the activationloop. Transphosphorylation of Tyrosine 493 by Lck leads to activation ofZap70. (Chan, et al 1995, Wange et al 1995, Mège, et al 1996) Thistyrosine residue corresponds to Tyrosine 1163 of the insulin receptorkinase domain which causes upon transphosphorylation, a majorconformational change of the activation loop (Hubbard 1997). It is thuslikely that the structure of the corresponding activation loop of ZAP-70phosphorylated at Tyrosine 493 will be different than the one shownhere. The role of Tyrosine 492 is less clear. A negative regulatoryfunction has been proposed (Chan, et al 1995). Tyrosine 474 is requiredfor association with the Shc adapter, which couples T cell receptorsignaling to the Ras pathway (Pacini, et al 1998). The surface exposedTyrosine 474 is located at the beginning of the β8 segment, close to thefollowing activation segment. Tyrosine 597 and 598 located at thesurface of the protein near to the C-terminus are supposed to beinvolved in regulating the functional activity of ZAP-70 possibly byinhibitory proteins (Zeitlmann, et al 1998). TABLE 1 Atomic Coordinatesof ZAP-70 catalytic Domain with Staurosporine REMARK 3 PROGRAM: CNX2000.1 REMARK 3 AUTHORS: Brunger, Adams, Clore, Delano, REMARK 3         Gros, Grosse-Kunstleve, Jiang, REMARK 3          Kuszewski,Nilges, Pannu, Read, REMARK 3          Rice, Simonson, Warren REMARK 3         and REMARK 3          Molecular Simulations Inc., REMARK 3         (Badger, Berard, Kumar, Szalma, REMARK 3          Yip). REMARK3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3  RESOLUTION RANGE HIGH(ANGSTROMS): 1.90 REMARK 3  RESOLUTION RANGE LOW  (ANGSTROMS): 19.26REMARK 3  DATA CUTOFF            (SIGMA(F)): 0.0 REMARK 3  DATA CUTOFFHIGH         (ABS(F)): 933984.58 REMARK 3  DATA CUTOFFLOW          (ABS(F)): 0.000000 REMARK 3  COMPLETENESS   (WORKING +TEST)(%): 96.7 REMARK 3  NUMBER OF REFLECTIONS: 45463 REMARK 3 REMARK 3 FITTO DATA USED IN REFINEMENT. REMARK 3  CROSS-VALIDATION METHOD:THROUGHOUT REMARK 3  FREE R VALUE TEST SET SELECTION: RANDOM REMARK 3  RVALUE (WORKING SET): 0.182 REMARK 3  FREE R VALUE: 0.209 REMARK 3  FREER VALUE TEST SET SIZE (%): 5.0 REMARK 3  FREE R VALUE TEST SET COUNT:2284 REMARK 3  ESTIMATED ERROR OF FREE R VALUE: 0.004 REMARK 3 REMARK 3FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3  TOTAL NUMBER OF BINS USED:6 REMARK 3  BIN RESOLUTION RANGE HIGH (A): 1.90 REMARK 3  BIN RESOLUTIONRANGE LOW (A): 2.02 REMARK 3  BIN COMPLETENESS (WORKING +TEST) (%): 93.7REMARK 3  REFLECTIONS IN BIN (WORKING SET): 6918 REMARK 3  BIN R VALUE(WORKING SET): 0.195 REMARK 3  BIN FREE R VALUE: 0.241 REMARK 3  BINFREE R VALUE TEST SET SIZE (%): 5.2 REMARK 3  BIN FREE R VALUE TEST SETCOUNT: 378 REMARK 3  ESTIMATED ERROR OF BIN FREE R VALUE: 0.012 REMARK 3REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS: 4739 REMARK 3  NUCLEIC ACID ATOMS: 0 REMARK 3  HETEROGENATOMS: 0 REMARK 3  SOLVENT ATOMS: 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) 24.1 REMARK 3  MEAN B VALUE (OVERALL, A**2)35.0 REMARK 3  OVERALL ANISOTROPIC B VALUE. REMARK 3  Bil (A**2): 0.16REMARK 3  B22 (A**2): −1.31 REMARK 3  B33 (A**2): 1.15 REMARK 3  B12(A**2): 0.00 REMARK 3  B13 (A**2): 2.08 REMARK 3  B23 (A**2): −1.25REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3  METHOD USED: FLATMODEL REMARK 3  KSOL: 0.38494 REMARK 3  BSOL: 52.9849 (A**2) REMARK 3REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3  ESD FROM LUZZATI PLOT(A): 0.19 REMARK 3  ESD FROM SIGMAA (A): 0.01 REMARK 3  LOW RESOLUTIONCUTOFF (A): 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATEERROR. REMARK 3  ESD FROM C-V LUZZATI PLOT (A): 0.22 REMARK 3  ESD FROMC-V SIGMAA       (A): 0.11 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEALVALUES. REMARK 3  BOND LENGTHS             (A): 0.011 REMARK 3  BONDANGLES        (DEGREES): 1.3 REMARK 3  DIHEDRAL ANGLES    (DEGREES):21.4 REMARK 3  IMPROPER ANGLES    (DEGREES): 0.91 REMARK 3 REMARK 3ISOTROPIC THERMAL MODEL: RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMALFACTOR RESTRAINTS. RMS   SIGMA REMARK 3  MAIN-CHAINBOND          (A**2): 3.56 ; 1.50 REMARK 3  MAIN-CHAINANGLE         (A**2): 4.55 ; 2.00 REMARK 3  SIDE-CHAINBOND          (A**2): 4.82 ; 2.00 REMARK 3  SIDE-CHAINANGLE         (A**2): 6.37 ; 2.50 REMARK 3 REMARK 3 NCS MODEL: NONEREMARK 3 REMARK 3 NCS RESTRAINTS. RMS  SIGMA/WEIGHT REMARK 3  GROUP 1POSITIONAL        (A) NULL ; NULL REMARK 3  GROUP 1B-FACTOR       (A**2) NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1:MSI_CNX_TOPPAR/proteinrep.param REMARK 3 PARAMETER FILE 2: MSI_10CNX_TOPPAR/waterrep.param REMARK 3 PARAMETER FILE 3: stu.param REMARK 3TOPOLOGY FILE 1: MSI_CNX_TOPPAR/protein.top REMARK 3 TOPOLOGY FILE 2:MSI_.CNX_TOPPAR/water.top REMARK 3 TOPOLOGY FILE 3: stu.toppar REMARK 3REMARK 3 OTHER REFINEMENT REMARKS: NULL SEQRES 1 A 273 PHE LEU LYS ARGASP ASN LEU LEU ILE ALA ASP ILE GLU SEQRES 2 A 273 LEU GLY CYS GLY ASNPHE GLY SER VAL ARG GLN GLY VAL SEQRES 3 A 273 TYR ARG MET ARG LYS LYSGLN ILE ASP VAL ALA ILE LYS SEQRES 4 A 273 VAL LEU LYS GLN GLY THR GLULYS ALA ASP THR GLU GLU SEQRES 5 A 273 MET MET ARG GLU ALA GLN ILE METHIS GLN LEU ASP ASN SEQRES 6 A 273 PRO TYR ILE VAL ARG LEU ILE GLY VALCYS GLN ALA GLU SEQRES 7 A 273 ALA LEU MET LEU VAL MET GLU MET ALA GLYGLY GLY PRO SEQRES 8 A 273 LEU HIS LYS PHE LEU VAL GLY LYS ARG GLU GLUILE PRO SEQRES 9 A 273 VAL SER ASN VAL ALA GLU LEU LEU HIS GLN VAL SERMET SEQRES 10 A 273 GLY MET LYS TYR LEU GLU GLU LYS ASN PHE VAL HIS ARGSEQRES 11 A 273 ASP LEU ALA ALA ARG ASN VAL LEU LEU VAL ASN ARG HISSEQRES 12 A 273 TYR ALA LYS ILE SER ASP PHE GLY LEU SER LYS ALA LEUSEQRES 13 A 273 GLY ALA ASP ASP SER TYR TYR THR ALA ARG SER ALA GLYSEQRES 14 A 273 LYS TRP PRO LEU LYS TRP TYR ALA PRO GLU CYS ILE ASNSEQRES 15 A 273 PHE ARG LYS PHE SER SER ARG SER ASP VAL TRP SER TYRSEQRES 16 A 273 GLY VAL THR MET TRP GLU ALA LEU SER TYR GLY GLN LYSSEQRES 17 A 273 PRO TYR LYS LYS MET LYS GLY PRO GLU VAL MET ALA PHESEQRES 18 A 273 ILE GLU GLN GLY LYS ARG MET GLU CYS PRO PRO GLU CYSSEQRES 19 A 273 PRO PRO GLU LEU TYR ALA LEU MET SER ASP CYS TRP ILESEQRES 20 A 273 TYR LYS TRP GLU ASP ARG PRO ASP PHE LEU THR VAL GLUSEQRES 21 A 273 GLN ARG MET ARG ALA CYS TYR TYR SER LEU ALA SER LYSSEQRES 1 B 273 PHE LEU LYS ARG ASP ASN LEU LEU ILE ALA ASP ILE GLUSEQRES 2 B 273 LEU GLY CYS GLY ASN PHE GLY SER VAL ARG GLN GLY VALSEQRES 3 B 273 TYR ARG MET ARG LYS LYS GLN ILE ASP VAL ALA ILE LYSSEQRES 4 B 273 VAL LEU LYS GLN GLY THR GLU LYS ALA ASP THR GLU GLUSEQRES 5 B 273 MET MET ARG GLU ALA GLN ILE MET HIS GLN LEU ASP ASNSEQRES 6 B 273 PRO TYR ILE VAL ARG LEU ILE GLY VAL CYS GLN ALA GLUSEQRES 7 B 273 ALA LEU MET LEU VAL MET GLU MET ALA GLY GLY GLY PROSEQRES 8 B 273 LEU HIS LYS PHE LEU VAL GLY LYS ARG GLU GLU ILE PROSEQRES 9 B 273 VAL SER ASN VAL ALA GLU LEU LEU HIS GLN VAL SER METSEQRES 10 B 273 GLY MET LYS TYR LEU GLU GLU LYS ASN PHE VAL HIS ARGSEQRES 11 B 273 ASP LEU ALA ALA ARG ASN VAL LEU LEU VAL ASN ARG HISSEQRES 12 B 273 TYR ALA LYS ILE SER ASP PHE GLY LEU SER LYS ALA LEUSEQRES 13 B 273 GLY ALA ASP ASP SER TYR TYR THR ALA ARG SER ALA GLYSEQRES 14 B 273 LYS TRP PRO LEU LYS TRP TYR ALA PRO GLU CYS ILE ASNSEQRES 15 B 273 PHE ARG LYS PHE SER SER ARG SER ASP VAL TRP SER TYRSEQRES 16 B 273 GLY VAL THR MET TRP GLU ALA LEU SER TYR GLY GLN LYSSEQRES 17 B 273 PRO TYR LYS LYS MET LYS GLY PRO GLU VAL MET ALA PHESEQRES 18 B 273 ILE GLU GLN GLY LYS ARG MET GLU CYS PRO PRO GLU CYSSEQRES 19 B 273 PRO PRO GLU LEU TYR ALA LEU MET SER ASP CYS TRP ILESEQRES 20 B 273 TYR LYS TRP GLU ASP ARG PRO ASP PHE LEU THR VAL GLUSEQRES 21 B 273 GLN ARG MET ARG ALA CYS TYR TYR SER LEU ALA SER LYSSEQRES 1 C   1 STU SEQRES 1 D   1 STU SEQRES 1 S 261 TIP TIP TIP TIP TIPTIP TIP TIP TIP TIP TIP TIP TIP SEQRES 2 S 261 TIP TIP TIP TIP TIP TIPTIP TIP TIP TIP TIP TIP TIP SEQRES 3 S 261 TIP TIP TIP TIP TIP TIP TIPTIP TIP TIP TIP TIP TIP SEQRES 4 S 261 TIP TIP TIP TIP TIP TIP TIP TIPTIP TIP TIP TIP TIP SEQRES 5 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIPTIP TIP TIP TIP SEQRES 6 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPTIP TIP TIP SEQRES 7 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPTIP TIP SEQRES 8 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPTIP SEQRES 9 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 10 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 11 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 12 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 13 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 14 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 15 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 16 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 17 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 18 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 19 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 20 S 261 TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIP TIPSEQRES 21 S 261 TIP CRYST 135.768   57.562   80.211   68.97   89.83   89.95   P 1   5 ORIGX 11.000000 0.000000 0.000000     0.00000 ORIGX 2 0.000000 1.0000000.000000     0.00000 ORIGX 3 0.000000 0.000000 1.000000     0.00000SCALE 1 0.027958 −0.000024 −0.000079     0.00000 SCALE 2 0.0000000.017373 −0.006679     0.00000 SCALE 3 0.000000 0.0000000.013357     0.00000 ATOM 1 CB PHE A 331 −0.844 −23.839 −13.860 1.0047.80 C ATOM 2 CG PHE A 331 −0.845 −24.256 −12.414 1.00 49.69 C ATOM 3CD1 PHE A 331 −2.033 −24.319 −11.699 1.00 53.17 C ATOM 4 CD2 PHE A 3310.342 −24.562 −11.764 1.00 47.25 C ATOM 5 CE1 PHE A 331 −2.041 −24.679−10.359 1.00 48.16 C ATOM 6 CE2 PHE A 331 0.344 −24.924 −10.421 1.0051.80 C ATOM 7 CZ PHE A 331 −0.849 −24.982 −9.720 1.00 49.42 C ATOM 8 CPHE A 331 −0.689 −21.905 −15.439 1.00 47.08 C ATOM 9 O PHE A 331 −1.461−21.795 −16.393 1.00 48.72 O ATOM 10 N PHE A 331 −2.670 −22.155 −13.9391.00 46.43 N ATOM 11 CA PHE A 331 −1.196 −22.366 −14.074 1.00 43.11 CATOM 12 N LEU A 332 0.610 −21.631 −15.514 1.00 40.15 N ATOM 13 CA LEU A332 1.245 −21.166 −16.746 1.00 42.89 C ATOM 14 CB LEU A 332 1.949−19.824 −16.490 1.00 42.08 C ATOM 15 CG LEU A 332 1.135 −18.662 −15.8941.00 41.32 C ATOM 16 CD1 LEU A 332 2.088 −17.561 −15.415 1.00 36.46 CATOM 17 CD2 LEU A 332 0.146 −18.116 −16.931 1.00 40.99 C ATOM 18 C LEU A332 2.273 −22.195 −17.207 1.00 41.99 C ATOM 19 O LEU A 332 2.746 −23.003−16.416 1.00 41.81 O ATOM 20 N LYS A 333 2.615 −22.171 −18.492 1.0042.98 N ATOM 21 CA LYS A 333 3.614 −23.091 −19.018 1.00 44.97 C ATOM 22CB LYS A 333 3.495 −23.221 −20.537 1.00 45.64 C ATOM 23 CG LYS A 3332.201 −23.857 −20.971 1.00 51.28 C ATOM 24 CD LYS A 333 2.310 −24.340−22.408 1.00 57.41 C ATOM 25 CE LYS A 333 1.041 −25.067 −22.838 1.0058.44 C ATOM 26 NZ LYS A 333 1.189 −25.656 −24.206 1.00 62.81 N ATOM 27C LYS A 333 4.998 22.577 −18.673 1.00 43.59 C ATOM 28 O LYS A 333 5.321−21.420 −18.952 1.00 39.19 O ATOM 29 N ARG A 334 5.813 −23.455 −18.0971.00 37.84 N ATOM 30 CA ARG A 334 7.167 −23.109 −17.698 1.00 42.87 CATOM 31 CB ARG A 334 7.831 −24.309 −17.015 1.00 46.05 C ATOM 32 CG ARG A334 9.264 −24.063 −16.553 1.00 41.63 C ATOM 33 CD ARG A 334 9.303−23.119 −15.368 1.00 37.46 C ATOM 34 NE ARG A 334 10.669 −22.817 −14.9471.00 37.67 N ATOM 35 CZ ARG A 334 11.471 −21.972 15.580 1.00 41.87 CATOM 36 NH1 ARG A 334 11.038 −21.340 −16.671 1.00 38.44 N ATOM 37 NH2ARG A 334 12.699 −21.747 −15.121 1.00 41.45 N ATOM 38 C ARG A 334 7.999−22.691 −18.905 1.00 42.10 C ATOM 39 O ARG A 334 8.981 −21.961 −18.7691.00 39.41 O ATOM 40 N ASP A 335 7.587 −23.169 −20.077 1.00 43.76 N ATOM41 CA ASP A 335 8.274 −22.895 −21.340 1.00 44.45 C ATOM 42 CB ASP A 3357.718 −23.822 −22.423 1.00 52.46 C ATOM 43 CG ASP A 335 7.632 −25.261−31.962 1.00 55.02 C ATOM 44 OD1 ASP A 335 8.688 −25.925 −21.897 1.0060.98 O ATOM 45 OD2 ASP A 335 6.512 −25.723 −21.643 1.00 62.85 O ATOM 46C ASP A 335 8.110 −21.455 −21.789 1.00 43.50 C ATOM 47 O ASP A 335 8.904−20.951 −22.594 1.00 41.39 O ATOM 48 N ASN A 336 7.079 −20.783 −21.2871.00 30.71 N ATOM 49 CA ASN A 336 6.837 −19.407 −21.673 1.00 33.27 CATOM 50 CB ASN A 336 5.341 −19.129 −31.723 1.00 36.84 C ATOM 51 CG ASN A336 4.647 −19.915 −22.809 1.00 49.26 C ATOM 52 OD1 ASN A 336 5.193−20.109 −23.899 1.00 49.53 O ATOM 53 ND2 ASN A 336 3.426 −20.351 −22.5271.00 48.43 N ATOM 54 C ASN A 336 7.494 −18.421 −20.731 1.00 28.53 C ATOM55 O ASN A 336 7.363 −17.210 −20.895 1.00 30.15 O ATOM 56 N LEU A 3378.203 −18.948 −19.749 1.00 32.36 N ATOM 57 CA LEU A 337 8.855 −18.115−18.750 1.00 34.27 C ATOM 58 CB LEU A 337 8.365 −18.518 −17.350 1.0030.14 C ATOM 59 CG LEU A 337 8.920 −17.781 −16.125 1.00 28.85 C ATOM 60CD1 LEU A 337 8.290 −16.416 −16.039 1.00 27.73 C ATOM 61 CD2 LEU A 3378.586 −18.559 −14.850 1.00 35.78 C ATOM 62 C LEU A 337 10.380 −18.202−18.800 1.00 31.60 C ATOM 63 O LEU A 337 10.956 −19.279 −18.875 1.0032.32 O ATOM 64 N LEU A 338 11.032 −17.051 −18.741 1.00 25.65 N ATOM 65CA LEU A 338 12.486 −17.006 −18.731 1.00 24.94 C ATOM 66 CB LEU A 33813.020 −16.257 −19.977 1.00 28.20 C ATOM 67 CG LEU A 338 14.554 −16.272−20.089 1.00 30.23 C ATOM 68 CD1 LEU A 338 15.028 −17.702 −20.306 1.0033.75 C ATOM 69 CD2 LEU A 338 15.012 −15.400 −21.245 1.00 31.10 C ATOM70 C LEU A 338 12.855 −16.235 −17.465 1.00 29.76 C ATOM 71 O LEU A 33812.624 −15.030 −17.384 1.00 30.99 O ATOM 72 N ILE A 339 13.401 −16.933−16.471 1.00 30.96 N ATOM 73 CA ILE A 339 13.763 −16.266 −15.219 1.0029.19 C ATOM 74 CB ILE A 339 13.645 −17.230 −14.011 1.00 33.77 C ATOM 75CG2 ILE A 339 13.921 −16.458 −13.704 1.00 30.52 C ATOM 76 CG1 ILE A 33912.267 −17.901 14.025 1.00 32.27 C ATOM 77 CD1 ILE A 339 12.057 −18.955−12.960 1.00 38.69 C ATOM 78 C ILE A 339 15.185 −15.743 −15.277 1.0031.14 C ATOM 79 O ILE A 339 16.119 −16.500 −15.534 1.00 34.19 O ATOM 80N ALA A 340 15.347 −14.448 −15.029 1.00 29.75 N ATOM 81 CA ALA A 34016.676 −13.843 −15.055 1.00 34.31 C ATOM 82 CB ALA A 340 16.569 −12.342−15.334 1.00 32.66 C ATOM 83 C ALA A 340 17.406 −14.090 −13.736 1.0036.59 C ATOM 84 O ALA A 340 16.788 −14.463 −12.724 1.00 34.25 O ATOM 85N ASP A 341 18.718 −13.901 −13.745 1.00 34.25 N ATOM 86 CA ASP A 34119.514 −14.093 −12.542 1.00 37.73 C ATOM 87 CA ASP A 341 20.924 −14.582−12.911 1.00 45.65 C ATOM 88 CG ASP A 341 21.639 −15.259 −11.738 1.0056.30 C ATOM 89 OD1 ASP A 341 21.455 −14.811 −10.588 1.00 59.09 O ATOM90 OD2 ASP A 341 22.399 −16.234 −11.966 1.00 62.33 O ATOM 91 C ASP A 34119.594 −12.739 −11.850 1.00 43.58 C ATOM 92 O ASP A 341 20.683 −12.245−11.562 1.00 44.94 O ATOM 93 N ILE A 342 18.434 −12.134 −11.595 1.0036.82 N ATOM 94 CA ILE A 342 18.349 −10.829 −10.954 1.00 35.58 C ATOM 95CB ILE A 342 17.894 −9.763 −11.969 1.00 38.49 C ATOM 96 CG2 ILE A 34217.708 −8.407 −11.281 1.00 43.25 C ATOM 97 CG1 ILE A 342 18.912 −9.675−13.106 1.00 36.31 C ATOM 98 CD1 ILE A 342 18.468 −8.769 −14.239 1.0046.83 C ATOM 99 C ILE A 342 17.327 −10.911 −9.825 1.00 37.22 C ATOM 100O ILE A 342 16.214 −11.364 −10.037 1.00 31.02 O ATOM 101 N GLU A 34317.710 −10.475 −8.633 1.00 33.59 N ATOM 102 CA GLU A 343 16.816 −10.526−7.485 1.00 36.18 C ATOM 103 CB GLU A 343 17.566 −11.064 −6.264 1.0036.52 C ATOM 104 CG GLU A 343 16.713 −11.123 −5.003 1.00 40.70 C ATOM105 CD GLU A 343 17.356 −11.929 −3.889 1.00 48.49 C ATOM 106 OE1 GLU A343 17.391 −13.175 −3.992 1.00 50.24 O ATOM 107 OE2 GLU A 343 17.833−11.314 −2.915 1.00 51.47 O ATOM 108 C GLU A 343 16.263 −9.143 −7.1801.00 37.22 C ATOM 109 O GLU A 343 17.031 −8.236 −6.890 1.00 32.38 O ATOM110 N LEU A 344 14.937 −8.989 −7.246 1.00 25.47 N ATOM 111 CA LEU A 34414.317 −7.693 −6.969 1.00 23.40 C ATOM 112 CB LEU A 344 12.916 −7.594−7.644 1.00 23.43 C ATOM 113 CG LEU A 344 12.969 −7.779 −9.161 1.0032.75 C ATOM 114 CD1 LEU A 344 11.538 −7.940 −9.704 1.00 27.03 C ATOM115 CD2 LEU A 344 13.684 −6.585 −9.819 1.00 32.92 C ATOM 116 C LEU A 34414.185 −7.494 −5.471 1.00 25.30 C ATOM 117 O LEU A 344 14.236 −6.365−4.982 1.00 29.77 O ATOM 118 N GLY A 345 13.997 −8.591 −4.736 1.00 25.68N ATOM 119 CA GLY A 345 13.884 −8.500 −3.296 1.00 27.74 C ATOM 120 C GLYA 345 13.777 −9.886 −2.700 1.00 29.98 C ATOM 121 O GLY A 345 13.835−10.872 −3.418 1.00 31.85 O ATOM 122 N CYS A 346 13.638 −9.976 −1.3821.00 29.57 N ATOM 123 CA CYS A 346 13.498 −11.286 −0.755 1.00 32.14 CATOM 124 CB CYS A 346 14.867 −11.885 −0.465 1.00 38.98 C ATOM 125 SG CYSA 346 15.741 −10.909 0.749 1.00 43.33 S ATOM 126 C CYS A 346 12.719−11.167 0.544 1.00 36.85 C ATOM 127 O CYS A 346 12.395 −10.063 0.9781.00 38.86 O ATOM 128 N GLY A 347 12.428 −12.316 1.142 1.00 36.28 N ATOM129 CA GLY A 347 11.704 −12.369 2.402 1.00 35.52 C ATOM 130 C GLY A 34711.923 −13.746 2.997 1.00 35.81 C ATOM 131 O GLY A 347 12.671 −14.5412.453 1.00 32.94 O ATOM 132 N ASN A 348 11.272 −14.040 4.116 1.00 39.18N ATOM 133 CA ASN A 348 11.406 −15.350 4.749 1.00 42.21 C ATOM 134 CBASN A 348 10.644 −15.387 6.080 1.00 48.61 C ATOM 135 CG ASN A 348 11.277−14.514 7.131 1.00 53.37 C ATOM 136 OD1 ASN A 348 12.422 −14.702 7.4921.00 56.08 O ATOM 137 ND2 ASN A 348 10.516 −13.546 7.635 1.00 59.19 NATOM 138 C ASN A 348 10.881 −16.464 3.852 1.00 39.31 C ATOM 139 O ASN A348 11.275 −17.619 3.996 1.00 39.22 O ATOM 140 N PHE A 349 9.980 −16.1162.933 1.00 35.86 N ATOM 141 CA PHE A 349 9.404 −17.095 2.016 1.00 32.64C ATOM 142 CB PHE A 349 8.143 −16.518 1.352 1.00 37.33 C ATOM 143 CG PHEA 349 8.416 −15.318 0.467 1.00 33.86 C ATOM 144 CD1 PHE A 349 9.019−15.475 −0.777 1.00 38.44 C ATOM 145 CD2 PHE A 349 8.121 −14.031 0.9051.00 37.11 C ATOM 146 CE1 PHE A 349 8.427 −14.360 −1.573 1.00 37.32 CATOM 147 CE2 PHE A 349 8.427 −12.917 0.123 1.00 38.27 C ATOM 148 CZ PHEA 349 9.036 −13.082 −1.120 1.00 36.15 C ATOM 149 C PHE A 349 10.394−17.491 0.919 1.00 33.34 C ATOM 150 O PHE A 349 10.333 −18.586 0.3671.00 36.04 O ATOM 151 N GLY A 350 11.287 −16.575 0.574 1.00 36.72 N ATOM152 CA GLY A 350 12.234 −16.848 −0.490 1.00 29.36 C ATOM 153 C GLY A 35012.627 −15.562 −1.166 1.00 32.07 C ATOM 154 O GLY A 350 12.959 −14.5910.506 1.00 37.38 O ATOM 155 N SER A 351 12.595 −15.526 −2.493 1.00 34.36N ATOM 156 CA SER A 351 12.993 −14.304 −3.151 1.00 33.56 C ATOM 157 CBSER A 351 14.439 −14.414 −3.605 1.00 39.89 C ATOM 158 OG SER A 35114.564 −15.336 −4.654 1.00 38.83 O ATOM 159 C SER A 351 12.093 −13.929−4.318 1.00 25.34 C ATOM 160 O SER A 351 11.246 −14.703 −4.741 1.0030.57 O ATOM 161 N VAL A 352 12.282 −12.719 −4.812 1.00 25.32 N ATOM 162CA VAL A 352 11.484 −12.243 −5.934 1.00 27.67 C ATOM 163 CB VAL A 35210.777 −10.928 −5.596 1.00 26.27 C ATOM 164 CG1 VAL A 352 9.988 −10.443−6.807 1.00 28.62 C ATOM 165 CG2 VAL A 352 9.846 −11.136 −4.387 1.0025.93 C ATOM 166 C VAL A 352 12.504 −12.002 −7.022 1.00 24.75 C ATOM 167O VAL A 352 13.416 −11.177 −6.862 1.00 26.64 O ATOM 168 N ARG A 35312.334 −12.720 −8.124 1.00 21.24 N ATOM 169 CA ARG A 353 13.259 −12.640−9.253 1.00 24.10 C ATOM 170 CB ARG A 353 13.643 −14.052 −9.721 1.0024.70 C ATOM 171 CG ARG A 353 14.430 −14.913 −8.722 1.00 41.94 C ATOM172 CD ARG A 353 15.851 −14.401 −8.516 1.00 48.67 C ATOM 173 NE ARG A353 16.805 −15.494 −8.339 1.00 56.82 N ATOM 174 CZ ARG A 353 17.287−16.243 −9.330 1.00 59.51 C ATOM 175 NH1 ARG A 353 16.913 −16.024−10.585 1.00 54.48 N ATOM 176 NH2 ARG A 353 18.140 −17.226 −9.065 1.0058.82 N ATOM 177 C ARG A 353 12.625 −11.910 −10.430 1.00 30.05 C ATOM178 O ARG A 353 11.403 −11.914 −10.605 1.00 32.28 O ATOM 179 N GLN A 35413.461 −11.288 −11.245 1.00 26.89 N ATOM 180 CA GLN A 354 12.954 −10.605−12.429 1.00 21.13 C ATOM 181 CB GLN A 354 13.886 −9.449 −12.813 1.0027.45 C ATOM 182 CG GLN A 354 13.394 −8.651 −14.005 1.00 33.20 C ATOM183 CD GLN A 354 14.196 −7.386 −14.228 1.00 35.81 C ATOM 184 OE1 GLN A354 14.929 −6.932 −13.344 1.00 32.36 O ATOM 185 NE2 GLN A 354 14.048−6.798 −15.410 1.00 38.36 N ATOM 186 C GLN A 354 12.954 −11.650 −13.5371.00 26.03 C ATOM 187 O GLN A 354 13.773 −12.580 −13.516 1.00 27.62 OATOM 188 N GLY A 355 12.044 −11.498 −14.498 1.00 23.59 N ATOM 189 CA GLYA 355 12.005 −12.421 −15.621 1.00 23.56 C ATOM 190 C GLY A 355 11.167−11.834 −16.740 1.00 28.28 C ATOM 191 O GLY A 355 10.786 −10.665 −16.7021.00 25.55 O ATOM 192 N VAL A 356 10.901 −12.664 −17.755 1.00 28.64 NATOM 193 CA VAL A 356 10.074 −12.264 −18.883 1.00 29.66 C ATOM 194 CBVAL A 356 10.921 −12.045 −20.174 1.00 34.30 C ATOM 195 CG1 VAL A 35610.005 −11.659 −21.351 1.00 32.44 C ATOM 196 CG2 VAL A 356 11.931−10.977 −19.919 1.00 29.39 C ATOM 197 C VAL A 356 9.108 −13.402 −19.1271.00 23.76 C ATOM 198 O VAL A 356 9.485 −14.569 −19.033 1.00 26.47 OATOM 199 N TYR A 357 7.859 −13.064 −19.438 1.00 28.83 N ATOM 200 CA TYRA 357 6.847 −14.082 −19.703 1.00 29.55 C ATOM 201 CB TYR A 357 5.697−14.003 −18.693 1.00 32.75 C ATOM 202 CG TYR A 357 4.603 −14.999 −18.9811.00 31.78 C ATOM 203 CD1 TYR A 357 4.766 −16.355 −18.702 1.00 33.06 CATOM 204 CE1 TYR A 357 3.761 −17.287 −19.010 1.00 38.12 C ATOM 205 CD2TYR A 357 3.47 −14.587 −19.575 1.00 38.71 C ATOM 206 CE2 TYR A 357 2.410−15.504 −19.887 1.00 39.65 C ATOM 207 CZ TYR A 357 2.587 −16.844 −19.6011.00 39.40 C ATOM 208 OH TYR A 357 1.577 −17.722 −19.904 1.00 48.05 OATOM 209 C TYR A 357 6.291 −13.846 −21.098 1.00 33.01 C ATOM 210 O TYR A357 6.038 −12.699 −21.484 1.00 34.42 O ATOM 211 N ARG A 358 6.093−14.925 −21.845 1.00 40.49 N ATOM 212 CA ARG A 358 5.582 −14.797 −23.2011.00 43.14 C ATOM 213 CB ARG A 358 6.303 −15.787 −24.128 1.00 42.64 CATOM 214 CG ARG A 358 5.804 −15.762 −25.580 1.00 47.94 C ATOM 215 CD ARGA 358 6.599 −16.738 −26.435 1.00 46.49 C ATOM 216 NE ARG A 358 7.470−19.024 26.159 1.00 47.27 N ATOM 217 CZ ARG A 358 7.470 −19.024 −26.1591.00 47.27 C ATOM 218 NH1 ARG A 358 8.496 −18.736 −26.947 1.00 48.46 NATOM 219 NH2 ARG A 358 7.365 −20.239 −25.636 1.00 49.08 N ATOM 220 C ARGA 358 4.083 −15.023 −23.299 1.00 37.81 C ATOM 221 O ARG A 358 3.602−16.102 −22.983 1.00 39.13 O ATOM 222 N MET A 359 3.361 −13.984 −23.7121.00 48.72 N ATOM 223 CA MET A 359 1.917 −14.072 −23.926 1.00 52.67 CATOM 224 CB MET A 359 1.185 −12.898 −23.284 1.00 56.85 C ATOM 225 CG META 359 1.487 −12.704 −21.817 1.00 59.91 C ATOM 226 SD MET A 359 0.442−11.450 −21.068 1.00 68.40 S ATOM 227 CE MET A 359 1.094 −9.949 −21.8451.00 66.35 C ATOM 228 C MET A 359 1.810 −13.963 −25.443 1.00 57.95 CATOM 229 O MET A 359 2.127 −13.913 −26.006 1.00 66.19 O ATOM 230 N ARG A360 1.393 −15.043 −26.097 1.00 60.89 N ATOM 231 CA ARG A 360 1.282−15.079 −27.561 1.00 63.37 C ATOM 232 CB ARG A 360 0.383 −16.246 −27.9941.00 64.54 C ATOM 233 CG ARG A 360 0.960 −17.616 −27.623 1.00 65.69 CATOM 234 CD ARG A 360 2.353 −17.786 −28.231 1.00 65.62 C ATOM 235 NE ARGA 360 3.255 −18.567 −27.384 1.00 65.60 N ATOM 236 CZ ARG A 360 3.082−19.851 −27.070 1.00 63.16 C ATOM 237 NH1 ARG A 360 2.027 −20.525−27.527 1.00 62.71 N ATOM 238 NH2 ARG A 360 3.977 −20.470 −26.309 1.0062.89 N ATOM 239 C ARG A 360 0.788 −13.774 −28.175 1.00 63.27 C ATOM 240O ARG A 360 −0.417 −13.601 −28.401 1.00 68.94 O ATOM 241 N LYS A 3611.743 −12.878 28.448 1.00 59.53 N ATOM 242 CA LYS A 361 1.511 −11.549−29.022 1.00 56.77 C ATOM 243 CB LYS A 361 0.219 −10.938 −28.461 1.0060.05 C ATOM 244 CG LYS A 361 0.226 −10.722 −26.950 1.00 60.48 C ATOM245 CD LYS A 361 −1.174 −10.402 −26.409 1.00 62.81 C ATOM 246 CE LYS A361 −1.771 −9.144 −27.036 1.00 64.09 C ATOM 247 NZ LYS A 361 −3.154−8.872 −26.526 1.00 65.39 N ATOM 248 C LYS A 361 2.701 −10.647 −28.6591.00 61.19 C ATOM 249 O LYS A 361 3.151 −9.813 −29.464 1.00 60.48 O ATOM250 N LYS A 362 3.204 −10.819 −27.436 1.00 52.69 N ATOM 251 CA LYS A 3624.334 −10.035 −26.949 1.00 54.92 C ATOM 252 CB LYS A 362 3.901 −8.588−26.737 1.00 56.85 C ATOM 253 CG LYS A 362 2.785 −8.432 −25.728 1.0053.56 C ATOM 254 CD LYS A 362 2.334 −6.986 −25.680 1.00 58.19 C ATOM 255CE LYS A 362 1.452 −6.738 −24.479 1.00 60.02 C ATOM 256 NZ LYS A 3620.281 −7.656 −24.462 1.00 59.99 C ATOM 257 C LYS A 362 4.900 −10.601−25.642 1.00 48.81 N ATOM 258 O LYS A 362 4.298 −11.460 −25.015 1.0048.05 C ATOM 259 N GLN A 362 6.069 −10.119 −25.241 1.00 51.22 O ATOM 260CA GLN A 363 6.682 −10.594 −24.007 1.00 49.77 N ATOM 261 CB GLN A 3638.095 −11.132 −24.267 1.00 54.46 C ATOM 262 CG GLN A 363 8.154 −12.259−25.286 1.00 52.95 C ATOM 263 CD GLN A 363 9.545 −12.865 −25.397 1.0054.97 C ATOM 264 OE1 GLN A 363 10.550 −12.189 −25.172 1.00 58.63 O ATOM265 NE2 GLN A 363 9.606 −14.135 −25.764 1.00 57.23 N ATOM 266 C GLN A363 6.737 −9.459 −23.014 1.00 46.14 C ATOM 267 O GLN A 363 7.198 −8.366−23.329 1.00 52.39 O ATOM 268 N GLN A 363 6.269 −9.716 −21.799 1.0038.56 N ATOM 269 CA ILE A 364 6.266 −8.671 −20.796 1.00 38.92 C ATOM 270CB ILE A 364 4.865 −8.450 −20.233 1.00 46.04 C ATOM 271 CG2 ILE A 3643.907 −8.072 −21.353 1.00 42.34 C ATOM 272 CG1 ILE A 364 4.388 −9.715−19.542 1.00 38.48 C ATOM 273 CD1 ILE A 364 3.262 −9.453 −18.591 1.0046.96 C ATOM 274 C ILE A 364 7.199 −8.974 −19.643 1.00 35.15 C ATOM 275O ILE A 364 7.473 −10.142 −19.337 1.00 29.70 O ATOM 276 N ASP A 3657.685 −7.922 −19.005 1.00 32.92 N ATOM 277 CA ASP A 365 8.577 −8.086−17.872 1.00 31.39 C ATOM 278 CB ASP A 365 9.253 −6.762 −17.522 1.0035.51 C ATOM 279 CG ASP A 365 10.142 −6.278 −18.685 1.00 40.87 C ATOM280 OD1 ASP A 365 10.983 −7.066 −19.158 1.00 44.73 O ATOM 281 OD2 ASP A365 9.997 −5.102 −19.089 1.00 47.04 O ATOM 282 C ASP A 365 7.728 −8.520−16.663 1.00 31.78 C ATOM 283 O ASP A 365 6.656 7.977 16.422 1.00 31.99O ATOM 284 N VAL A 366 8.214 −9.484 −15.889 1.00 25.27 N ATOM 285 CA VALA 366 7.472 −9.945 −14.722 1.00 24.77 C ATOM 286 CB VAL A 366 6.831−11.346 14.959 1.00 21.57 C ATOM 287 CG1 VAL A 366 5.761 −11.282 −16.0551.00 23.23 C ATOM 288 CG2 VAL A 366 7.923 −12.389 −15.281 1.00 24.77 CATOM 289 C VAL A 366 8.365 −10.061 −13.486 1.00 26.20 C ATOM 290 O VAL A366 9.576 −10.016 −13.580 1.00 26.40 O ATOM 291 N ALA A 367 7.742−10.156 −12.315 1.00 23.36 N ATOM 292 CA ALA A 367 8.471 −10.354 −11.0741.00 27.38 C ATOM 293 CB ALA A 367 8.166 −9.227 −10.067 1.00 25.34 CATOM 294 C ALA A 367 7.911 −11.716 −10.615 1.00 29.93 C ATOM 295 O ALA A367 6.703 −11.961 −10.667 1.00 29.39 O ATOM 296 N ILE A 368 8.799−12.603 −10.203 1.00 26.23 N ATOM 297 CA ILE A 368 8.418 −13.962 −9.8141.00 26.26 C ATOM 298 CB ILE A 368 9.182 −15.008 −10.677 1.00 29.25 CATOM 299 CG2 ILE A 368 8.711 −16.425 −10.355 1.00 27.48 C ATOM 300 CG1ILE A 368 8.974 −14.706 −12.168 1.00 26.91 C ATOM 301 CD1 ILE A 36810.261 −14.543 −12.965 1.00 35.91 C ATOM 302 C ILE A 368 8.744 −14.257−8.352 1.00 26.03 C ATOM 303 O ILE A 368 9.893 −14.229 −7.959 1.00 24.27O ATOM 304 N LYS A 369 7.720 −14.539 −7.561 1.00 25.90 N ATOM 305 CA LYSA 369 7.953 −14.862 −6.156 1.00 26.26 C ATOM 306 CB LYS A 369 6.691−14.547 −5.344 1.00 25.23 C ATOM 307 CG LYS A 369 6.822 −14.795 −3.8701.00 31.86 C ATOM 308 CD LYS A 369 5.509 −14.423 −3.158 1.00 34.03 CATOM 309 CE LYS A 369 5.438 −14.876 −1.716 1.00 39.65 C ATOM 310 NZ LYSA 369 4.354 −14.402 −0.910 1.00 31.37 N ATOM 311 C LYS A 369 8.298−16.361 −6.140 1.00 27.61 C ATOM 312 O LYS A 369 7.474 −17.219 −6.4921.00 29.29 O ATOM 313 N VAL A 370 9.532 −16.674 −5.764 1.00 26.60 N ATOM314 CA VAL A 370 9.990 −18.065 −5.766 1.00 28.07 C ATOM 315 CB VAL A 37011.355 −18.200 −6.481 1.00 33.07 C ATOM 316 CG1 VAL A 370 11.721 −19.667−6.633 1.00 38.83 C ATOM 317 CG2 VAL A 370 11.315 −17.506 −7.841 1.0030.80 C ATOM 318 C VAL A 370 10.154 −18.575 −4.340 1.00 33.33 C ATOM 319O VAL A 370 10.920 −18.021 −3.558 1.00 31.84 O ATOM 320 N LEU A 3719.433 −19.627 −3.996 1.00 32.52 N ATOM 321 CA LEU A 371 9.555 −20.176−2.653 1.00 37.90 C ATOM 322 CB LEU A 371 8.383 −21.111 −2.357 1.0040.40 C ATOM 323 CG LEU A 371 7.003 −20.462 −2.304 1.00 38.75 C ATOM 324CD1 LEU A 371 5.960 −21.529 −2.018 1.00 42.86 C ATOM 325 CD2 LEU A 3716.987 −19.389 −1.236 1.00 40.03 C ATOM 326 C LEU A 371 10.877 −20.936−2.523 1.00 41.99 C ATOM 327 O LEU A 371 11.250 −21.709 −3.413 1.0037.51 O ATOM 328 N LYS A 372 11.517 −20.717 −1.411 1.00 40.63 N ATOM 329CA LYS A 372 12.847 −21.374 −1.151 1.00 47.85 C ATOM 330 CB LYS A 37213.430 −20.879 0.176 1.00 49.15 C ATOM 331 CG LYS A 372 12.538 −21.1281.390 1.00 52.08 C ATOM 332 CD LYS A 372 13.153 −20.548 2.655 1.00 53.51C ATOM 333 CE LYS A 372 12.283 −20.840 3.875 1.00 55.66 C ATOM 334 NZLYS A 372 12.885 −20.313 5.137 1.00 59.56 N ATOM 335 C LYS A 372 12.691−22.894 −1.121 1.00 52.35 C ATOM 336 O LYS A 372 11.591 −23.413 −0.9411.00 50.37 O ATOM 337 N GLN A 373 13.799 −23.605 −1.312 1.00 59.78 NATOM 338 CA GLN A 373 13.780 −25.067 −1.304 1.00 59.32 C ATOM 339 CB GLNA 373 15.115 −25.606 −1.835 1.00 63.62 C ATOM 340 CG GLN A 373 15.155−27.116 −2.051 1.00 66.24 C ATOM 341 CD GLN A 373 14.191 −27.586 −3.1341.00 71.01 C ATOM 342 OE1 GLN A 373 12.970 −27.465 −2.995 1.00 69.21 OATOM 343 NE2 GLN A 373 14.739 −28.129 −4.219 1.00 68.75 N ATOM 344 C GLNA 373 13.529 −25.584 0.116 1.00 60.87 C ATOM 345 O GLN A 373 14.088−25.061 1.085 1.00 58.13 O ATOM 346 N GLY A 374 12.673 −26.595 0.2381.00 60.47 N ATOM 347 CA GLY A 374 12.378 −27.150 1.548 1.00 63.49 CATOM 348 C GLY A 374 11.112 −26.589 2.169 1.00 65.45 C ATOM 349 O GLY A374 10.744 −26.960 3.287 1.00 64.91 O ATOM 350 N THR A 375 10.448−25.694 1.440 1.00 64.08 N ATOM 351 CA THR A 375 9.211 −25.073 1.9101.00 62.35 C ATOM 352 CB THR A 375 8.624 −24.117 0.837 1.00 61.07 C ATOM353 OG1 THR A 375 9.499 −22.997 0.658 1.00 58.51 O ATOM 354 CG2 THR A375 7.251 −23.619 1.255 1.00 60.44 C ATOM 355 C THR A 375 8.164 −26.1282.254 1.00 60.26 C ATOM 356 O THR A 375 7.812 −26.960 1.420 1.00 61.11 OATOM 357 N GLU A 376 7.669 −26.085 3.486 1.00 61.48 N ATOM 358 CA GLU A376 6.659 −27.038 3.937 1.00 63.66 C ATOM 359 CB GLU A 376 6.395 −26.8545.431 1.00 65.34 C ATOM 360 CG GLU A 376 5.410 −27.863 6.011 1.00 70.83C ATOM 361 CD GLU A 376 5.443 −27.905 7.531 1.00 74.17 C ATOM 362 OE1GLU A 376 5.151 −26.868 8.174 1.00 71.51 O ATOM 363 OE2 GLU A 376 5.765−28.983 8.083 1.00 74.47 0 ATOM 364 C GLU A 376 5.365 −26.847 3.157 1.0064.69 C ATOM 365 O GLU A 376 5.071 −25.745 2.693 1.00 62.88 O ATOM 366 NLYS A 377 4.595 −27.921 3.015 1.00 60.06 N ATOM 367 CA LYS A 377 3.339−27.860 2.282 1.00 61.26 C ATOM 368 CB LYS A 377 2.637 −29.219 2.3171.00 66.02 C ATOM 369 CG LYS A 377 1.309 −29.238 1.575 1.00 65.91 C ATOM370 CD LYS A 377 0.916 −30.656 1.195 1.00 71.13 C ATOM 371 CE LYS A 377−0.343 −30.679 0.335 1.00 69.84 C ATOM 372 NZ LYS A 377 −0.745 −32.070−0.037 1.00 70.61 N ATOM 373 C LYS A 377 2.405 −26.794 2.833 1.00 60.41C ATOM 374 O LYS A 377 1.535 −26.293 2.121 1.00 58.25 O ATOM 375 C ALA A378 2.586 −26.456 4.104 1.00 60.36 N ATOM 376 CA ALA A 378 1.757 −25.4504.756 1.00 60.42 C ATOM 377 CB ALA A 378 2.126 −25.353 6.232 1.00 60.96C ATOM 378 C ALA A 378 1.914 −24.083 4.090 1.00 58.57 C ATOM 379 O ALA A378 0.928 −23.406 3.792 1.00 58.22 O ATOM 380 N ASP A 379 3.159 −23.6903.849 1.00 58.14 N ATOM 381 CA ASP A 379 3.446 −22.398 3.237 1.00 59.61C ATOM 382 CB ASP A 379 4.889 −21.999 3.513 1.00 61.20 C ATOM 383 CG ASPA 379 5.387 −22.533 4.841 1.00 69.25 C ATOM 384 OD1 ASP A 379 4.801−22.184 5.892 1.00 70.24 O ATOM 385 OD2 ASP A 379 6.367 −23.313 4.8311.00 70.38 O ATOM 386 C ASP A 379 3.198 −22.428 1.730 1.00 57.10 C ATOM387 O ASP A 379 2.944 −21.394 1.118 1.00 54.39 O ATOM 388 N THR A 3803.279 −23.616 1.137 1.00 51.67 N ATOM 389 CA THR A 380 3.023 −23.766−0.287 1.00 52.52 C ATOM 390 CB THR A 380 3.350 −25.193 −0.755 1.0053.17 C ATOM 391 OG1 THR A 380 4.769 −25.392 −0.709 1.00 55.35 O ATOM392 CG2 THR A 380 2.858 −25.411 −2.168 1.00 57.49 C ATOM 393 C THR A 3801.536 −23.488 −0.506 1.00 53.07 C ATOM 394 O THR A 380 1.142 −22.808−1.449 1.00 46.30 O ATOM 395 N GLU A 381 0.714 −24.029 0.386 1.00 48.31N ATOM 396 CA GLU A 381 −0.726 −23.844 0.310 1.00 49.46 C ATOM 397 CBGLU A 381 −1.421 −24.722 1.355 1.00 55.95 C ATOM 398 CG GLU A 381 −2.487−25.651 0.794 1.00 57.87 C ATOM 399 CD GLU A 381 −1.909 −26.852 0.0641.00 66.85 C ATOM 400 OE1 GLU A 381 −1.256 −26.663 −0.988 1.00 67.42 OATOM 401 OE2 GLU A 381 −2.112 −27.992 0.547 1.00 68.23 O ATOM 402 C GLUA 381 −1.025 −22.371 0.585 1.00 47.48 C ATOM 403 O GLU A 381 −1.985−21.810 0.061 1.00 44.28 O ATOM 404 N GLU A 382 −0.181 −21.752 1.4041.00 42.74 N ATOM 405 CA GLU A 382 −0.332 −20.346 1.764 1.00 44.98 CATOM 406 CB GLU A 382 0.697 −19.989 2.828 1.00 50.35 C ATOM 407 CG GLU A382 0.552 −18.600 3.407 1.00 54.73 C ATOM 408 CD GLU A 382 1.479 −18.3764.593 1.00 61.59 C ATOM 409 OE1 GLU A 382 2.719 −18.344 4.400 1.00 67.89O ATOM 410 OE2 GLU A 382 0.963 −18.241 5.726 1.00 66.58 O ATOM 411 C GLUA 382 −0.150 −19.453 0.531 1.00 43.95 C ATOM 412 O GLU A 382 −0.893−18.490 0.331 1.00 37.04 O ATOM 413 N MET A 383 0.847 −19.772 −0.2881.00 38.03 N ATOM 414 CA MET A 383 1.063 −18.984 −1.490 1.00 37.01 CATOM 415 CB MET A 383 2.425 −19.295 −2.124 1.00 37.76 C ATOM 416 CG META 383 2.854 −18.195 −3.108 1.00 44.12 C ATOM 417 SD MET A 383 4.495−18.400 −3.806 1.00 45.79 S ATOM 418 CE MET A 383 4.148 −19.720 −4.8491.00 27.93 C ATOM 419 C MET A 383 −0.054 −19.244 −2.490 1.00 33.92 CATOM 420 O MET A 383 −0.365 −18.389 −3.311 1.00 28.10 O ATOM 421 N MET A384 0.672 −20.423 −2.432 1.00 30.29 N ATOM 422 CA MET A 384 −1.770−20.707 −3.346 1.00 35.41 C ATOM 423 CB MET A 384 −2.129 −22.190 −3.3381.00 37.28 C ATOM 424 CG MET A 384 −1.098 −23.082 −4.013 1.00 44.29 CATOM 425 SD MET A 384 −0.753 −22.611 −5.733 1.00 47.70 S ATOM 426 CE META 384 −2.394 −22.740 −6.491 1.00 43.44 C ATOM 427 C MET A 384 −2.988−19.871 −2.970 1.00 32.30 C ATOM 428 O MET A 384 −3.746 −19.436 −3.8381.00 32.40 O ATOM 429 N ARG A 385 −3.186 −19.642 −1.680 1.00 36.42 NATOM 430 CA ARG A 385 −4.305 −18.814 −1.250 1.00 36.70 C ATOM 431 CB ARGA 385 −4.470 −18.850 0.270 1.00 41.37 C ATOM 432 CG ARG A 385 −5.158−20.106 0.794 1.00 46.84 C ATOM 433 CD ARG A 385 −5.569 −19.933 2.2611.00 45.50 C ATOM 434 NE ARG A 385 −4.432 −20.021 3.171 1.00 49.04 NATOM 435 CZ ARG A 385 −3.842 −21.165 3.508 1.00 48.50 C ATOM 436 NH1 ARGA 385 −4.291 −22.309 3.007 1.00 48.28 N ATOM 437 NH2 ARG A 385 −2.806−21.167 4.334 1.00 48.88 N ATOM 438 C ARG A 385 −4.048 −17.381 −1.7121.00 32.36 C ATOM 439 O ARG A 385 −4.970 −16.666 −2.088 1.00 34.82 OATOM 440 N GLU A 386 −2.780 −16.976 −1.692 1.00 29.93 N ATOM 441 CA GLUA 386 −2.780 −15.633 −2.125 1.00 29.40 C ATOM 442 CB GLU A 386 −0.893−15.413 −1.881 1.00 28.50 C ATOM 443 CG GLU A 386 −0.333 −14.053 −2.2891.00 33.73 C ATOM 444 CD GLU A 386 1.178 −13.959 −2.037 1.00 35.02 CATOM 445 OE1 GLU A 386 1.750 −14.956 −1.548 1.00 36.68 O ATOM 446 OE2GLU A 386 1.797 −12.905 −2.343 1.00 36.70 O ATOM 447 C GLU A 386 −2.713−15.481 −3.615 1.00 27.47 C ATOM 448 O GLU A 386 −3.215 −14.437 −4.0601.00 28.61 O ATOM 449 N ALA A 387 −2.412 −16.525 −4.377 1.00 30.23 NATOM 450 CA ALA A 387 −2.673 −16.488 −5.806 1.00 33.30 C ATOM 451 CB ALAA 387 −2.097 −17.735 −6.484 1.00 32.95 C ATOM 452 C ALA A 387 −4.194−16.386 −6.031 1.00 30.92 C ATOM 453 O ALA A 387 −4.638 −15.601 −6.8431.00 33.56 O ATOM 454 N GLN A 388 −4.975 −17.163 −5.286 1.00 31.73 NATOM 455 CA GLN A 388 −6.440 −17.119 −6.438 1.00 36.88 C ATOM 456 CB GLNA 388 −7.108 −18.109 −4.461 1.00 36.88 C ATOM 457 CG GLN A 388 −6.725−19.564 −4.694 1.00 48.53 C ATOM 458 CD GLN A 388 −7.273 −20.496 −3.6191.00 55.51 C ATOM 459 OE1 GLN A 388 −8.480 −20.524 −3.360 1.00 58.01 OATOM 460 NE2 GLN A 388 −6.383 =21.263 −2.982 1.00 52.09 N ATOM 461 C GLNA 388 −7.001 −15.711 −5.201 1.00 33.60 C ATOM 462 O GLN A 388 −7.904−15.271 −5.902 1.00 O ATOM 463 N ILE A 389 −6.469 −15.004 −4.204 1.0030.12 N ATOM 464 CA ILE A 389 −6.914 −13.643 −3.905 1.00 25.06 C ATOM465 CB ILE A 389 −6.305 −13.132 −2.569 1.00 28.76 C ATOM 466 CG2 ILE A389 −6.507 −11.626 −2.426 1.00 29.47 C ATOM 467 CG1 ILE A 389 −6.964−13.868 −1.398 1.00 37.06 C ATOM 468 CD1 ILE A 389 −6.359 −13.540 −0.0581.00 34.67 C ATOM 469 C ILE A 389 −6.524 −12.696 −5.022 1.00 26.55 CATOM 470 O ILE A 389 −7.326 −11.901 −5.494 1.00 30.71 O ATOM 471 N MET A390 −5.278 −12.779 −5.461 1.00 27.33 N ATOM 472 CA MET A 390 −4.845−11.910 −6.529 1.00 24.55 C ATOM 473 CB MET A 390 −3.353 −12.085 −6.8091.00 24.16 C ATOM 474 CG MET A 390 −2.457 −11.523 −5.714 1.00 24.68 CATOM 475 SD MET A 390 −0.694 −11.770 −6.180 1.00 31.52 S ATOM 476 CE META 390 −0.450 −10.325 −7.210 1.00 31.50 C ATOM 477 C MET A 390 −5.638−12.215 −7.807 1.00 29.46 C ATOM 478 O MET A 390 −5.960 −11.302 −8.5581.00 30.11 O ATOM 479 N HIS A 391 −5.945 −13.493 −8.024 1.00 30.83 NATOM 480 CA HIS A 391 −6.689 −13.890 −9.230 1.00 37.84 C ATOM 481 CB HISA 391 −6.738 −15.420 −9.340 1.00 43.52 C ATOM 482 CG HIS A 391 −7.283−15.921 −10.645 1.00 49.94 C ATOM 483 CD2 HIS A 391 −6.657 −16.380−11.756 1.00 51.86 C ATOM 484 ND1 HIS A 391 −8.633 −15.956 −10.924 1.0055.85 N ATOM 485 CE1 HIS A 391 −8.816 −16.416 −12.149 1.00 15.35 C ATOM486 NE2 HIS A 391 −7.634 −16.681 −12.675 1.00 57.80 N ATOM 487 C HIS A391 −8.106 −13.321 −9.231 1.00 42.10 C ATOM 488 O HIS A 391 −8.778−13.315 −10.262 1.00 47.79 O ATOM 489 N GLN A 392 −8.559 −12.839 −8.0771.00 39.91 N ATOM 490 CA GLN A 392 −9.898 −12.259 −7.965 1.00 41.34 CATOM 491 CB GLN A 392 −10.543 −12.659 −6.633 1.00 43.83 C ATOM 492 CGGLN A 392 −10.631 −14.161 −6.437 1.00 47.90 C ATOM 493 CD GLN A 392−11.399 −14.548 −5.197 1.00 51.89 C ATOM 494 OE1 GLN A 392 −12.612−14.361 −5.124 1.00 58.95 O ATOM 495 NE2 GLN A 392 −10.699 −15.095−4.210 1.00 51.91 N ATOM 496 C GLN A 392 −9.860 −10.742 −8.067 1.0046.24 C ATOM 497 O GLN A 392 −10.888 −10.081 −7.932 1.00 43.30 O ATOM498 N LEU A 393 −8.676 −10.190 −8.317 1.00 43.90 N ATOM 499 CA LEU A 393−8.511 −8.741 −8.416 1.00 43.71 C ATOM 500 CB LEU A 393 −7.350 −8.287−7.530 1.00 46.31 C ATOM 501 CG LEU A 393 −7.356 −8.772 −6.080 1.0047.53 C ATOM 502 CD1 LEU A 393 −6.097 −8.274 −5.384 1.00 44.78 C ATOM503 CD2 LEU A 393 −8.601 −8.278 −5.364 1.00 38.33 C ATOM 504 C LEU A 393−8.269 −8.257 −9.843 1.00 45.51 C ATOM 505 O LEU A 393 −7.485 −8.847−10.597 1.00 50.21 O ATOM 506 N ASP A 394 −8.924 −7.167 −10.220 1.0041.60 N ATOM 507 CA ASP A 394 −8.759 6.638 −11.565 1.00 38.62 C ATOM 508CB ASP A 394 −9.874 −7.175 −12.473 1.00 45.48 C ATOM 509 CG ASP A 394−9.733 −6.718 −13.917 1.00 53.93 C ATOM 510 OD1 ASP A 394 −10.609 −7.075−14.740 1.00 54.65 O ATOM 511 OD2 ASP A 394 −8.756 −6.009 −14.235 1.0049.40 O ATOM 512 C ASP A 394 −8.821 −5.132 −11.499 1.00 41.64 C ATOM 513O ASP A 394 −9.870 −4.523 −11.744 1.00 41.10 O ATOM 514 N ASN A 395−7.692 −4.519 −11.169 1.00 38.06 N ATOM 515 CA ASN A 395 −7.654 −3.07511.057 1.00 29.93 C ATOM 516 CB ASN A 395 −7.902 −2.678 −9.592 1.0027.46 C ATOM 517 CG ASN A 395 −8.027 −1.187 −9.397 1.00 34.86 C ATOM 518OD1 ASN A 395 −9.106 −0.602 −9.581 1.00 38.20 O ATOM 519 ND2 ASN A 395−6.923 −0.552 −9.025 1.00 25.87 N ATOM 520 C ASN A 395 −6.285 −2.610−11.530 1.00 30.95 C ATOM 521 O ASN A 395 −5.258 −3.260 −11.269 1.0028.17 O ATOM 522 N PRO A 396 −6.248 −1.467 −12.222 1.00 28.97 N ATOM 523CD PRO A 396 −7.395 −0.706 −12.748 1.00 39.56 C ATOM 524 CA PRO A 396−4.996 −0.919 −12.733 1.00 28.79 C ATOM 525 CB PRO A 396 −5.464 0.277−13.556 1.00 37.29 C ATOM 526 CG PRO A 396 −6.842 −0.149 −14.019 1.0042.13 C ATOM 527 C PRO A 396 −3.997 −0.494 −11.656 1.00 28.11 C ATOM 528O PRO A 396 −2.821 −0.352 −11.939 1.00 27.45 O ATOM 529 N TYR A 397−4.471 −0.298 −10.422 1.00 24.07 N ATOM 530 CA TYR A 397 −3.576 0.171−9.346 1.00 22.72 C ATOM 531 CB TYR A 397 −4.250 1.346 −8.618 1.00 21.97C ATOM 532 CG TYR A 397 −4.655 2.442 −9.593 1.00 25.66 C ATOM 533 CD1TYR A 397 −5.994 2.640 −9.946 1.00 29.62 C ATOM 534 CE1 TYR A 397 −6.3563.604 −10.886 1.00 34.32 C ATOM 535 CD2 TYR A 397 −3.689 3.238 −10.2061.00 25.78 C ATOM 536 CE2 TYR A 397 −4.044 4.206 −11.152 1.00 36.01 CATOM 537 CZ TYR A 397 −5.376 4.380 −11.490 1.00 37.11 C ATOM 538 OH TYRA 397 −5.694 4.380 −11.490 1.00 37.11 O ATOM 539 C TYR A 397 −3.127−0.896 −8.368 1.00 21.63 C ATOM 540 O TYR A 397 −2.730 −0.615 −7.2131.00 23.29 O ATOM 541 N ILE A 398 −3.193 −2.125 −8.832 1.00 22.86 N ATOM542 CA ILE A 398 −2.770 −3.266 −8.069 1.00 29.14 C ATOM 543 CB ILE A 398−4.005 −4.065 −7.641 1.00 34.44 C ATOM 544 CG2 ILE A 398 −3.602 −5.424−7.156 1.00 37.06 C ATOM 545 CG1 ILE A 398 −4.768 −3.273 −6.575 1.0028.40 C ATOM 546 CD1 ILE A 398 −6.166 −3.759 −6.305 1.00 41.40 C ATOM547 C ILE A 398 −1.858 −4.102 −8.975 1.00 33.99 C ATOM 548 O ILE A 3998−2.096 −4.193 −10.183 1.00 34.40 O ATOM 549 N VAL A 399 −0.805 −4.672−8.402 1.00 27.19 N ATOM 550 CA VAL A 399 0.109 −5.540 −9.155 1.00 26.99C ATOM 551 CB VAL A 399 1.298 −6.006 −8.302 1.00 29.43 C ATOM 552 CG1VAL A 399 2.078 −7.146 −9.026 1.00 26.20 C ATOM 553 CG2 VAL A 399 2.200−4.832 −8.031 1.00 30.03 C ATOM 554 C VAL A 399 −0.704 −6.759 −9.5391.00 33.87 C ATOM 555 O VAL A 399 −1.162 −7.498 −8.670 1.00 35.03 O ATOM556 N ARG A 400 −0.849 −6.986 −10.837 1.00 26.00 N ATOM 557 CA ARG A 400−1.652 −8.098 −11.315 1.00 30.60 C ATOM 558 CB ARG A 400 −2.172 −7.785−12.728 1.00 38.54 C ATOM 559 CG ARG A 400 −3.035 −6.521 −12.854 1.0046.40 C ATOM 560 CD ARG A 400 −3.410 −6.240 −14.331 1.00 46.44 C ATOM561 NE ARG A 400 −4.269 −5.066 −14.505 1.00 52.85 N ATOM 562 CZ ARG A400 −5.554 −5.032 −14.163 1.00 56.01 C ATOM 563 NH1 ARG A 400 −6.117−6.110 −13.633 1.00 52.93 N ATOM 564 NH2 ARG A 400 −6.276 −3.928 −14.3461.00 53.59 N ATOM 565 C ARG A 400 −0.946 −9.444 −11.324 1.00 27.57 CATOM 566 O ARG A 400 0.257 −9.548 −11.572 1.00 27.90 O ATOM 567 N LEU A401 −1.703 −10.500 −11.077 1.00 28.32 N ATOM 568 CA LEU A 401 −1.147−11.838 −11.096 1.00 24.81 C ATOM 569 CB LEU A 401 −1.974 −12.777−10.238 1.00 32.19 C ATOM 570 CG LEU A 401 −1.534 −14.239 −10.271 1.0029.13 C ATOM 571 CD1 LEU A 401 −0.159 −14.414 −9.638 1.00 37.61 C ATOM572 CD2 LEU A 401 −2.578 −15.046 −9.516 1.00 42.15 C ATOM 573 C LEU A401 −1.194 −12.352 −12.525 1.00 32.86 C ATOM 574 O LEU A 401 −2.248−12.281 −13.176 1.00 30.25 O ATOM 575 N ILE A 402 −0.060 −12.831 −13.0261.00 26.16 N ATOM 576 CA ILE A 402 −0.031 −13.405 −14.364 1.00 28.41 CATOM 577 CB ILE A 402 1.394 −13.397 −14.987 1.00 29.05 C ATOM 578 CG2ILE A 402 1.360 −14.080 −16.360 1.00 33.43 C ATOM 579 CG1 ILE A 4021.898 −11.957 −15.135 1.00 28.86 C ATOM 580 CD1 ILE A 402 0.925 −11.026−15.810 1.00 33.60 C ATOM 581 C ILE A 402 −0.508 −14.853 −14.187 1.0031.32 C/ ATOM 582 O ILE A 402 −1.402 −15.330 −14.890 1.00 29.93 O ATOM583 N GLY A 403 0.070 −15.548 −13.224 1.00 29.11 N ATOM 584 CA GLY A 403−0.335 −16.924 −12.971 1.00 28.71 C ATOM 585 C GLY A 403 0.639 −17.626−12.060 1.00 28.89 C ATOM 586 O GLY A 403 1.605 −17.020 −11.612 1.0029.79 O ATOM 587 N VAL A 404 0.387 −18.900 −11.787 1.00 27.61 N ATOM 588CA VAL A 404 1.259 −19.697 −10.938 1.00 31.08 C ATOM 589 CB VAL A 4040.436 −20.508 −9.911 1.00 36.46 C ATOM 590 CG1 VAL A 404 1.360 −21.378−9.052 1.00 42.77 C ATOM 591 CG2 VAL A 404 −0.370 −19.564 −9.051 1.0037.69 C ATOM 592 C VAL A 404 2.019 −20.671 −11.283 1.00 29.99 C ATOM 593O VAL A 404 1.480 −21.154 −12.802 1.00 32.94 O ATOM 594 N CYS A 4053.262 −20.969 −11.461 1.00 31.70 N ATOM 595 CA CYS A 405 4.065 −21.908−12.243 1.00 37.20 C ATOM 596 CB CYS A 405 5.131 −21.150 −13.042 1.0040.22 C ATOM 597 SG CYS A 405 5.968 −22.154 −14.282 1.00 46.07 S ATOM598 C CYS A 405 4.717 −22.939 −11.324 1.00 40.66 C ATOM 599 O CYS A 4055.428 −22.587 −10.388 1.00 39.23 O ATOM 600 N GLN A 406 4.453 −24.213−11.583 1.00 40.69 N ATOM 601 CA GLN A 406 5.011 −25.282 −10.762 1.0050.34 C ATOM 602 CB GLN A 406 3.900 −26.245 −10.326 1.00 53.46 C ATOM603 CG GLN A 406 4.373 −27.347 −9.486 1.00 59.61 C ATOM 604 CD GLN A 4065.156 −27.032 −8.240 1.00 55.65 C ATOM 605 OE1 GLN A 406 6.329 −26.665−8.316 1.00 61.62 O ATOM 606 NE2 GLN A 406 4.504 −27.099 −7.088 1.0058.42 N ATOM 607 C GLN A 406 6.090 −26.044 −11.519 1.00 53.49 C ATOM 608O GLN A 406 5.792 −26.902 −12.345 1.00 56.41 O ATOM 609 N ALA A 4077.342 −25.718 −11.234 1.00 54.94 N ATOM 610 CA ALA A 407 8.468 −26.378−11.879 1.00 59.69 C ATOM 611 CB ALA A 407 9.105 −25.437 −12.902 1.0059.62 C ATOM 612 C ALA A 407 9.484 −26.782 −10.811 1.00 57.77 C ATOM 613O ALA A 407 9.173 −27.578 −9.923 1.00 57.65 O ATOM 614 N GLU A 40810.692 −26.232 −10.895 1.00 54.86 N ATOM 615 CA GLU A 408 11.730 −26.541−9.921 1.00 56.21 C ATOM 616 CB GLU A 408 13.002 −25.738 −10.220 1.0060.73 C ATOM 617 CG GLU A 408 12.777 −24.237 −10.370 1.00 60.37 C ATOM618 CD GLU A 408 12.597 −23.801 −11.818 1.00 61.95 C ATOM 619 OE1 GLU A408 11.749 −24.377 −12.535 1.00 61.59 O ATOM 620 OE2 GLU A 408 13.308−22.866 −12.238 1.00 60.74 O ATOM 621 C GLU A 408 11.216 −26.210 −8.5241.00 57.49 C ATOM 622 O GLU A 408 11.766 −26.663 −7.517 1.00 60.01 OATOM 623 N ALA A 409 10.155 −25.411 −8.480 1.00 56.44 N ATOM 624 CA ALAA 409 9.519 −25.007 −7.231 1.00 52.91 C ATOM 625 CB ALA A 409 10.480−24.178 −6.392 1.00 58.00 C ATOM 626 C ALA A 409 8.276 −24.196 −7.5891.00 49.70 C ATOM 627 O ALA A 409 8.029 −23.822 −8.750 1.00 46.56. OATOM 628 N LEU A 410 7.420 −23.942 −6.601 1.00 48.39 N ATOM 629 CA LEU A410 6.189 −23.192 −6.830 1.00 42.60 C ATOM 630 CB LEU A 410 5.210−23.433 −5.681 1.00 42.05 C ATOM 631 CG LEU A 410 3.794 −22.949 −5.9681.00 39.06 C ATOM 632 CD1 LEU A 410 3.256 −23.669 −7.199 1.00 42.72 CATOM 633 CD2 LEU A 410 2.912 −23.207 −4.752 1.00 46.20 C ATOM 634 C LEUA 410 6.516 −21.711 −6.941 1.00 34.88 C ATOM 635 O LEU A 410 7.246−21.714 −6.118 1.00 32.97 O ATOM 636 N MET A 411 5.969 −21.052 −7.9561.00 32.78 N ATOM 637 CA MET A 411 6.269 −19.647 −8.171 1.00 27.80 CATOM 638 CB MET A 411 7.272 −19.506 −9.326 1.00 29.67 C ATOM 639 CG META 411 8.546 −20.333 −9.200 1.00 37.85 C ATOM 640 SD MET A 411 9.647−20.153 −10.644 1.00 40.33 S ATOM 641 CE MET A 411 8.672 −20.909 −11.8591.00 38.19 C ATOM 642 C MET A 411 5.024 −18.846 −8.521 1.00 29.61 C ATOM643 O MET A 411 4.126 −19.354 −9.171 1.00 32.53 O ATOM 644 N LEU A 4124.975 −17.593 −8.083 1.00 26.11 N ATOM 645 CA LEU A 412 3.864 −16.704−8.426 1.00 23.60 C ATOM 646 CB LEU A 412 3.340 −15.957 −7.197 1.0030.66 C ATOM 647 CG LEU A 412 2.475 −16.741 −6.224 1.00 43.14 C ATOM 648CD1 LEU A 412 1.856 −15.774 −5.208 1.00 39.76 C ATOM 649 CD2 LEU A 4121.389 −17.457 −7.018 1.00 42.58 C ATOM 650 C LEU A 412 4.450 −15.688−9.391 1.00 33.31 C ATOM 651 O LEU A 412 5.348 −14.947 −9.004 1.00 24.93O ATOM 652 N VAL A 413 3.928 −15.663 −10.626 1.00 26.19 N ATOM 653 CAVAL A 413 4.385 −14.739 −11.674 1.00 24.01 C ATOM 654 CB VAL A 413 4.374−15.425 −13.070 1.00 25.63 C ATOM 655 CG1 VAL A 413 4.951 −14.465−14.143 1.00 22.85 C ATOM 656 CG2 VAL A 413 5.192 −16.718 −13.010 1.0026.67 C ATOM 657 C VAL A 413 3.458 −13.540 −11.700 1.00 26.19 C ATOM 658O VAL A 413 2.240 −13.673 −11.925 1.00 28.56 O ATOM 659 N MET A 4144.052 −12.368 −11.490 1.00 22.49 N ATOM 660 CA MET A 414 3.324 −11.108−11.418 1.00 22.14 C ATOM 661 CB MET A 414 3.422 −10.545 −9.987 1.0025.30 C ATOM 662 CG MET A 414 2.767 −11.409 −8.917 1.00 28.88 C ATOM 663SD MET A 414 3.377 −10.874 −7.264 1.00 30.85 S ATOM 664 CE MET A 4144.890 −11.872 −7.109 1.00 32.45 C ATOM 665 C MET A 414 3.871 −10.049−12.336 1.00 34.63 C ATOM 666 O MET A 414 5.017 −10.131 −12.796 1.0025.46 O ATOM 667 N GLU A 415 3.075 −9.012 −12.568 1.00 25.97 N ATOM 668CA GLU A 415 3.548 −7.913 −13.395 1.00 25.91 C ATOM 669 CB GLU A 4152.470 −6.842 −13.568 1.00 37.31 C ATOM 670 CG GLU A 415 1.181 −7.321−14.191 1.00 41.51 C ATOM 671 CD GLU A 415 0.151 −6.190 −14.258 1.0056.50 C ATOM 672 OE1 GLU A 415 −0.056 −5.493 −13.222 1.00 39.84 O AOTM673 OE2 GLU A 415 −0.444 −5.998 −15.346 1.00 55.15 O ATOM 674 C GLU A415 4.711 07.273 −12.651 1.00 26.45 C ATOM 675 O GLU A 415 4.751 −7.287−12.651 1.00 26.92 O ATOM 676 N MET A 416 5.657 −6.713 −13.400 1.0027.12 N ATOM 677 CA MET A 416 6.784 −6.047 −12.778 1.00 26.18 C ATOM 678CB MET A 416 8.078 −6.047 −12.778 1.00 29.98 C ATOM 679 CG MET A 4169.308 −5.885 −12.729 1.00 32.43 C ATOM 680 SD MET A 416 10.835 −6.141−13.631 1.00 40.73 S ATOM 681 CE MET A 416 11.931 −4.939 −12.809 1.0040.48 C ATOM 682 C MET A 416 6.577 −4.539 −12.781 1.00 30.68 C ATOM 683O MET A 416 6.117 −3.981 −13.766 1.00 29.07 O ATOM 684 N ALA A 417 6.916−3.893 −11.670 1.00 28.26 N ATOM 685 CA ALA A 417 6.843 −2.436 −11.5611.00 31.40 C ATOM 686 CB ALA A 417 5.886 −2.023 −11.253 1.00 31.37 CATOM 687 C ALA A 417 8.286 −2.023 −11.253 1.00 31.10 C ATOM 688 O ALA A417 8.672 −1.865 −10.087 1.00 31.97 O ATOM 689 N GLY A 418 9.064 −1.876−12.330 1.00 35.10 N ATOM 690 CA GLY A 418 10.485 1.554 −12.258 1.0034.74 C ATOM 691 C GLY A 418 10.936 −0.340 −11.474 1.00 32.22 C ATOM 692O GLY A 418 12.120 −0.205 −11.147 1.00 33.36 O ATOM 693 N GLY A 41910.002 0.559 −11.183 1.00 26.94 N ATOM 694 CA GLY A 419 10.354 1.740−10.421 1.00 27.31 C ATOM 695 C GLY A 419 10.674 1.386 −8.978 1.00 27.31C ATOM 696 O GLY A 419 11.321 2.150 −8.287 1.00 31.61 O ATOM 697 N GLY A420 10.196 0.235 −8.506 1.00 32.29 N ATOM 698 CA GLY A 420 10.469 −0.166−7.139 1.00 27.34 C ATOM 699 C GLY A 420 9.632 0.511 −6.054 1.00 27.22 CATOM 700 O GLY A 420 8.709 1.263 −6.369 1.00 25.34 O ATOM 701 N PRO A421 9.952 0.280 −4.770 1.00 27.85 N ATOM 702 CD PRO A 421 11.122 −0.509−4.330 1.00 29.71 C ATOM 703 CA PRO A 421 9.247 0.843 −3.612 1.00 25.99C ATOM 704 CB PRO A 421 10.049 0.310 −2.411 1.00 33.47 C ATOM 705 CG PROA 421 10.755 −0.872 −2.921 1.00 33.83 C ATOM 706 C PRO A 421 9.178 2.358−3.574 1.00 32.23 C ATOM 707 O PRO A 421 10.126 3.052 03.845 1.00 25.70O ATOM 708 N LEU A 422 8.002 2.856 −3.196 1.00 24.75 N ATOM 709 CA LEU A422 7.726 4.280 −3.094 1.00 24.74 C ATOM 710 CB LEU A 422 6.258 4.475−2.705 1.00 25.86 C ATOM 711 CG LEU A 422 5.736 5.899 −2.536 1.00 27.46C ATOM 712 CD1 LEU A 422 5.749 6.599 −3.879 1.00 29.48 C ATOM 713 CD2LEU A 422 4.322 5.851 −1.989 1.00 26.17 C ATOM 714 C LEU A 422 8.6075.010 −2.078 1.00 24.09 C ATOM 715 O LEU A 422 9.065 6.128 −2.347 1.0027.09 O ATOM 716 N HIS A 423 8.821 4.423 −0.908 1.00 23.84 N ATOM 717 CAHIS A 423 9.627 5.097 0.097 1.00 31.59 C ATOM 718 CB HIS A 423 9.6774.309 1.410 1.00 33.34 C ATOM 719 CG HIS A 423 10.255 2.935 1.274 1.0032.56 C ATOM 720 CD2 HIS A 423 10.263 2.066 0.236 1.00 33.97 C ATOM 721ND1 HIS A 423 10.947 2.318 2.296 1.00 40.55 N ATOM 722 CE1 HIS A 42311.355 1.128 1.894 1.00 33.85 C ATOM 723 NE2 HIS A 423 10.952 0.9500.647 1.00 37.19 N ATOM 724 C HIS A 423 11.048 5.352 −0.417 1.00 35.72 CATOM 725 O HIS A 423 11.583 6.444 −0.235 1.00 38.98 O ATOM 726 N LYS A424 11.647 4.356 −1.064 1.00 26.67 N ATOM 727 CA LYS A 424 13.000 4.559−1.576 1.00 30.40 C ATOM 728 CB LYS A 424 13.625 3.217 −1.950 1.00 30.75C ATOM 729 CG LYS A 424 13.884 2.327 −0.747 1.00 32.42 C ATOM 730 CD LYSA 424 14.486 0.996 −1.191 1.00 42.37 C ATOM 731 CE LYS A 424 14.6350.035 −0.020 1.00 47.25 C ATOM 732 NZ LYS A 424 15.606 −1.054 −0.3601.00 54.40 N ATOM 733 C LYS A 424 13.025 5.500 −2.767 1.00 30.87 C ATOM734 O LYS A 424 13.976 6.259 −2.944 1.00 27.95 O ATOM 735 N PHE A 42511.975 5.479 −3.586 1.00 27.56 N ATOM 736 CA PHE A 425 11.919 6.345−4.755 1.00 27.56 C ATOM 737 CB PHE A 425 10.693 6.006 −5.612 1.00 33.85C ATOM 738 CG PHE A 425 10.536 6.885 −6.816 1.00 33.08 C ATOM 739 CD1PHE A 425 11.259 6.634 −7.976 1.00 43.47 C ATOM 740 CD2 PHE A 425 9.6927.986 −6.778 1.00 38.10 C ATOM 741 CE1 PHE A 425 11.146 7.476 −9.0831.00 42.11 C ATOM 742 CE2 PHE A 425 9.567 8.832 −7.874 1.00 47.88 C ATOM743 CZ PHE A 425 10.297 8.574 −9.033 1.00 44.70 C ATOM 744 C PHE A 42511.861 7.838 −4.391 1.00 29.42 C ATOM 745 O PHE A 425 12.421 8.681−5.097 1.00 27.18 O ATOM 746 N LEU A 426 11.198 8.174 −3.295 1.00 26.78N ATOM 747 CA LEU A 426 11.053 9.581 −2.919 1.00 23.65 C ATOM 748 CB LEUA 426 9.750 9.793 −2.142 1.00 23.99 C ATOM 749 CG LEU A 426 8.484 9.543−2.972 1.00 23.37 C ATOM 750 CD1 LEU A 426 7.234 9.646 −2.081 1.00 23.77C ATOM 751 CD2 LEU A 426 8.429 10.547 −4.096 1.00 27.33 C ATOM 752 C LEUA 426 12.210 10.161 −2.100 1.00 29.71 C ATOM 753 O LEU A 426 12.34511.379 −2.011 1.00 24.55 O ATOM 754 N VAL A 427 13.021 9.296 −1.501 1.0025.47 N ATOM 755 CA VAL A 427 14.130 9.781 −0.661 1.00 28.99 C ATOM 756CB VAL A 427 14.996 8.607 −0.132 1.00 34.76 C ATOM 757 CG1 VAL A 42716.250 9.148 0.578 1.00 37.93 C ATOM 758 CG2 VAL A 427 14.186 7.7620.852 1.00 30.76 C ATOM 759 C VAL A 427 15.027 10.780 −1.403 1.00 34.84C ATOM 760 O VAL A 427 15.605 10.464 −2.445 1.00 37.55 O ATOM 761 N GLYA 428 15.117 11.993 −0.862 1.00 43.08 N ATOM 762 CA GLY A 428 15.94113.030 −1.469 1.00 41.65 C ATOM 763 C GLY A 428 15.437 13.634 −2.7681.00 47.74 C ATOM 764 O GLY A 428 16.196 14.303 −3.479 1.00 42.77 O ATOM765 N LYS A 429 14.163 13.430 −3.090 1.00 37.30 N ATOM 766 CA LYS A 42913.624 13.972 −4.328 1.00 41.14 C ATOM 767 CB LYS A 429 13.024 12.840−5.161 1.00 46.03 C ATOM 768 CG LYS A 429 14.064 11.799 −5.568 1.0046.82 C ATOM 769 CD LYS A 429 13.607 11.007 −6.775 1.00 54.33 C ATOM 770CE LYS A 429 14.575 9.879 −7.099 1.00 52.59 C ATOM 771 NZ LYS A 42914.028 9.018 −8.182 1.00 61.02 N ATOM 772 C LYS A 429 12.596 15.079−4.098 1.00 43.46 C ATOM 773 O LYS A 429 11.741 15.347 −4.952 1.00 46.64O ATOM 774 N ARG A 430 12.696 15.736 −2.950 1.00 38.34 N ATOM 775 CA ARGA 430 11.765 16.798 −2.604 1.00 51.71 C ATOM 776 CB ARG A 430 12.05017.298 −1.189 1.00 53.36 C ATOM 777 CG ARG A 430 10.922 18.125 −0.5911.00 62.96 C ATOM 778 CD ARG A 430 11.039 18.217 0.928 1.00 63.14 C ATOM779 NE ARG A 430 9.729 18.100 1.576 1.00 52.24 N ATOM 780 CZ ARG A 4309.526 17.461 2.724 1.00 68.34 C ATOM 781 NH1 ARG A 430 10.545 16.8903.355 1.00 63.91 N ATOM 782 NH2 ARG A 430 8.293 17.358 3.231 1.00 65.90N ATOM 783 C ARG A 430 11.818 17.957 −3.591 1.00 54.65 C ATOM 784 O ARGA 430 10.867 18.723 −3.716 1.00 53.09 O ATOM 785 N GLU A 431 12.93218.078 −4.307 1.00 55.81 N ATOM 786 CA GLU A 431 13.077 19.158 −5.2681.00 54.84 C ATOM 787 CB GLU A 431 14.428 19.855 −5.092 1.00 58.53 CATOM 788 CG GLU A 431 14.491 20.755 −3.869 1.00 61.42 C ATOM 789 CD GLUA 431 15.662 21.716 −3.910 1.00 67.37 C ATOM 790 OE1 GLU A 431 15.71522.555 −4.841 1.00 71.67 O ATOM 791 OE2 GLU A 431 16.530 21.638 −3.0131.00 68.85 O ATOM 792 C GLU A 431 12.913 18.709 −6.705 1.00 55.28 C ATOM793 O GLU A 431 12.995 19.521 −7.622 1.00 58.15 O ATOM 794 N GLU A 43212.678 17.420 −6.912 1.00 50.44 N ATOM 795 CA GLU A 432 12.498 16.923−8.263 1.00 48.35 C ATOM 796 CB GLU A 432 13.596 15.918 −8.623 1.0055.95 C ATOM 797 CG GLU A 432 13.285 14.477 −8.287 1.00 55.95 C ATOM 798CD GLU A 432 14.264 13.513 −8.934 1.00 62.60 C ATOM 799 OE1 GLU A 43215.463 13.571 −8.594 1.00 66.37 O ATOM 800 OE2 GLU A 432 13.837 12.700−9.786 65.64 O ATOM 801 C GLU A 432 11.125 16.285 −8.432 1.00 47.94 CATOM 802 O GLU A 432 10.661 16.082 −9.548 1.00 47.37 O ATOM 803 N ILE A433 10.474 15.968 −7.315 1.00 39.35 N ATOM 804 CA ILE A 433 9.143 15.364−7.361 1.00 35.26 C ATOM 805 CB ILE A 433 9.148 13.942 −6.758 1.00 40.43C ATOM 806 CG2 ILE A 433 7.742 13.332 −6.819 1.00 32.65 C ATOM 807 CG1ILE A 433 10.120 13.056 −7.527 1.00 39.75 C ATOM 808 CD1 ILE A 433 9.72012.837 −8.964 1.00 41.51 C ATOM 809 C ILE A 433 8.252 16.258 −6.521 1.0036.84 C ATOM 810 O ILE A 433 8.276 16.182 −5.291 1.00 32.85 O ATOM 811 NPRO A 434 7.467 17.134 −7.172 1.00 33.02 N ATOM 812 CD PRO A 434 7.51017.400 −8.618 1.00 41.68 C ATOM 813 CA PRO A 434 6.554 18.074 −6.5121.00 36.57 C ATOM 814 CB PRO A 434 5.925 18.812 −7.693 1.00 37.02 C ATOM815 CG PRO A 434 7.033 18.833 −8.679 1.00 47.39 C ATOM 816 C PRO A 4345.512 17.377 −5.648 1.00 31.45 C ATOM 817 O PRO A 434 5.227 16.199−5.848 1.00 28.84 O ATOM 818 N VAL A 435 4.944 18.121 −4.702 1.00 32.88N ATOM 819 CA VAL A 435 3.919 17.568 −3.821 1.00 34.12 C ATOM 820 CB VALA 435 3.457 18.619 −2.777 1.00 32.16 C ATOM 821 CG1 VAL A 435 2.33518.041 −1.904 1.00 32.92 C ATOM 822 CG2 VAL A 435 4.629 19.012 −1.9011.00 39.50 C ATOM 823 C VAL A 435 2.731 17.093 −4.642 1.00 34.03 C ATOM824 O VAL A 435 2.096 16.076 −4.299 1.00 26.73 O ATOM 825 N SER A 4362.424 17.821 −5.721 1.00 27.34 N ATOM 826 CA SER A 436 1.321 17.445−6.595 1.00 26.52 C ATOM 827 CB SER A 436 1.152 18.482 −7.752 1.00 34.16C ATOM 828 OG SER A 436 2.339 18.588 −8.494 1.00 36.95 O ATOM 829 C SERA 436 1.517 16.038 −7.187 1.00 29.26 C ATOM 830 O SER A 436 0.548 15.298−7.359 1.00 28.55 O ATOM 831 N ASN A 437 2.763 15.676 −7.486 1.00 24.99N ATOM 832 CA ASN A 437 3.085 14.372 −8.060 1.00 24.95 C ATOM 833 CB ASNA 437 4.499 14.432 −8.649 1.00 30.76 C ATOM 834 CG ASN A 437 4.89113.192 −9.462 1.00 33.40 C ATOM 835 OD1 ASN A 437 5.922 13.209 −10.1401.00 31.35 O ATOM 836 ND2 ASN A 437 4.107 12.116 −9.381 1.00 33.64 NATOM 837 C ASN A 437 2.957 13.330 −6.923 1.00 24.92 C ATOM 838 O ASN A437 2.472 12.224 −7.133 1.00 26.65 O ATOM 839 N VAL A 438 3.371 13.695−5.719 1.00 25.75 N ATOM 840 CA VAL A 438 3.201 12.755 −4.612 1.00 24.63C ATOM 841 CB VAL A 438 3.819 13.291 −3.321 1.00 28.75 C ATOM 842 CG1VAL A 438 3.496 12.348 −2.162 1.00 25.61 C ATOM 843 CG2 VAL A 438 5.33813.426 −3.500 1.00 27.56 C ATOM 844 C VAL A 438 1.697 12.523 −4.409 1.0024.68 C ATOM 845 O VAL A 438 1.277 11.391 −4.258 1.00 22.54 O ATOM 846 NALA A 439 0.888 13.591 −4.441 1.00 22.86 N ATOM 847 CA ALA A 439 −0.56713.437 −4.280 1.00 25.85 C ATOM 848 CB ALA A 439 −1.263 14.843 −4.2171.00 25.16 C ATOM 849 C ALA A 439 −1.188 12.589 −5.395 1.00 22.87 C ATOM850 O ALA A 439 −2.146 11.861 −5.154 1.00 23.17 O ATOM 851 N GLU A 440−0.647 12.685 −6.614 1.00 21.21 N ATOM 852 CA GLU A 440 −1.157 11.900−7.728 1.00 25.32 C ATOM 853 CB GLU A 440 −0.380 12.246 −9.014 1.0030.55 C ATOM 854 CG GLU A 440 −0.636 11.301 −10.184 1.00 29.05 C ATOM855 CD GLU A 440 0.286 11.582 −11.368 1.00 40.39 C ATOM 856 OE1 GLU A440 1.448 11.984 −11.145 1.00 35.18 O ATOM 857 OE2 GLU A 440 −0.15111.385 −12.523 1.00 36.07 O ATOM 858 C GLU A 440 −0.998 10.404 −7.4061.00 31.15 C ATOM 859 O GLU A 440 −1.923 9.614 −7.585 1.00 23.98 O ATOM860 N LEU A 441 0.181 10.035 −6.913 1.00 24.24 N ATOM 861 CA LEU A 4410.500 8.646 −6.573 1.00 21.78 C ATOM 862 CB LEU A 441 1.991 8.541 −6.2221.00 22.41 C ATOM 863 CG LEU A 441 2.937 8.916 −7.366 1.00 22.95 C ATOM864 CD1 LEU A 441 4.389 8.882 −6.901 1.00 27.25 C ATOM 865 CD2 LEU A 4412.720 7.939 −8.521 1.00 19.84 C ATOM 866 C LEU A 441 −0.354 8.186 −5.3771.00 18.04 C ATOM 867 O LEU A 441 −0.872 7.067 −5.375 1.00 23.44 O ATOM868 N LEU A 442 −0.476 9.040 −4.369 1.00 20.94 N ATOM 869 CA LEU A 442−1.310 8.653 −3.219 1.00 24.86 C ATOM 870 CB LEU A 442 −1.233 9.698−2.115 1.00 22.54 C ATOM 871 CG LEU A 442 0.100 9.753 −1.362 1.00 22.80C ATOM 872 CD1 LEU A 442 0.125 10.921 −0..55 1.00 22.67 C ATOM 873 CD2LEU A 442 0.315 8.398 −0.661 1.00 23.13 C ATOM 874 C LEU A 442 −2.7618.469 −3.667 1.00 25.24 C ATOM 875 O LEU A 442 −3.454 7.581 −3.187 1.0022.68 O ATOM 876 N HIS A 443 −3.228 9.290 −4.605 1.00 23.39 N ATOM 877CA HIS A 443 −4.607 9.115 −5.069 1.00 22.12 C ATOM 878 CB HIS A 443−5.024 10.280 −5.985 1.00 27.77 C ATOM 879 CG HIS A 443 −6.388 10.101−6.573 1.00 28.68 C ATOM 880 CD2 HIS A 443 −7.565 9.739 −6.004 1.0027.01 C ATOM 881 ND1 HIS A 443 −6.628 10.196 −7.929 1.00 24.79 N ATOM882 CE1 HIS A 443 −7.893 9.897 −8.171 1.00 24.33 C ATOM 883 NE2 HIS A443 −8.484 9.613 −7.021 1.00 22.99 N ATOM 884 C HIS A 443 −4.781 7.762−5.781 1.00 22.67 C ATOM 885 O HIS A 443 −5.792 7.077 −5.600 1.00 21.81O ATOM 886 N GLN A 444 −3.791 7.354 −6.569 1.00 22.84 N ATOM 887 CA GLNA 444 −3.855 6.076 −7.251 1.00 18.98 C ATOM 888 CB GLN A 444 −2.6375.909 −8.152 1.00 23.77 C ATOM 889 CG GLN A 444 −2.679 6.923 −9.303 1.0023.82 C ATOM 890 CD GLN A 444 −1.445 6.867 −10.130 1.00 29.64 C ATOM 891OE1 GLN A 444 −0.424 6.344 −9.697 1.00 28.87 O ATOM 892 NE2 GLN A 444−1.521 7.419 −11.342 1.00 28.75 N ATOM 893 C GLN A 444 −3.911 4.958−6.218 1.00 21.47 C ATOM 894 O GLN A 444 −4.682 4.029 −6.354 1.00 22.83O ATOM 895 N VAL A 445 −3.114 5.094 −5.162 1.00 21.95 N ATOM 896 CA VALA 445 −3.162 4.075 −4.119 1.00 19.79 C ATOM 897 CB VAL A 445 −2.1314.359 −3.001 1.00 21.17 C ATOM 898 CG1 VAL A 445 −2.309 3.326 −1.8621.00 22.83 C ATOM 899 CG2 VAL A 445 −0.732 4.274 −3.575 1.00 19.35 CATOM 900 C VAL A 445 −4.576 4.070 −3.510 1.00 20.72 C ATOM 901 O VAL A445 −5.107 3.002 −3.225 1.00 21.91 O ATOM 902 N SER A 446 −5.184 5.244−3.316 1.00 18.98 N ATOM 903 CA SER A 446 −6.543 5.260 −2.734 1.00 19.98C ATOM 904 CB SER A 446 −6.988 6.704 −2.353 1.00 21.69 C ATOM 905 OG SERA 446 −7.327 7.481 −3.468 1.00 24.84 O ATOM 906 C SER A 446 −7.573 4.627−3.662 1.00 20.82 C ATOM 907 O SER A 446 −8.553 4.037 −3.187 1.00 21.15O ATOM 908 N MET A 447 −7.366 4.714 −4.974 1.00 19.01 N ATOM 909 CA META 447 −8.294 4.078 −5.909 1.00 22.58 C ATOM 910 CB MET A 447 −8.0714.588 −7.347 1.00 23.29 C ATOM 911 CG MET A 447 −8.540 6.039 −7.513 1.0027.40 C ATOM 912 SD MET A 447 −8.500 6.538 −9.288 1.00 29.46 S ATOM 913CE MET A 447 −6.769 6.928 −9.496 1.00 28.17 C ATOM 914 C MET A 447−8.133 2.558 −5.838 1.00 25.02 C ATOM 915 O MET A 447 −9.114 1.821−5.859 1.00 22.91 O ATOM 916 N GLY A 448 −6.903 2.076 −5.729 1.00 20.29N ATOM 917 CA GLY A 448 −6.712 0.644 −5.625 1.00 22.77 C ATOM 918 C GLYA 448 −7.337 0.135 −4.327 1.00 23.66 C ATOM 919 O GLY A 448 −7.963−0.934 −4.331 1.00 24.13 0 ATOM 920 N MET A 449 −7.192 0.892 −3.236 1.0022.40 N ATOM 921 CA MET A 449 −7.756 0.450 −1.939 1.00 21.23 C ATOM 922CB MET A 449 −7.139 1.232 −0.775 1.00 20.57 C ATOM 923 CG MET A 449−5.611 1.012 0.550 1.00 19.53 C ATOM 924 SD MET A 449 −5.170 0.771 0.3821.00 25.09 S ATOM 925 CE MET A 449 −6.110 −1.175 1.087 1.00 26.33 C ATOM926 C MET A 449 −9.282 0.566 −1.888 1.00 22.12 C ATOM 927 O MET A 449−9.964 0.236 −1.245 1.00 22.36 O ATOM 928 N LYS A 450 −9.832 1.554−2.578 1.00 21.36 N ATOM 929 CA LYS A 450 −11.276 1.705 −2.642 1.0024.95 C ATOM 930 CB LYS A 450 −11.616 2.949 −3.457 1.00 24.95 C ATOM 931CG LYS A 450 −13.113 3.108 −3.668 1.00 34.59 C ATOM 932 CD LYS A 450−13.388 4.170 −4.678 1.00 35.54 C ATOM 933 CE LYS A 450 −14.854 4.088−5.081 1.00 43.28 C ATOM 934 NZ LYS A 450 −15.200 5.226 −5.962 1.0051.23 N ATOM 935 C LYS A 450 −11.811 0.436 −3.328 1.00 20.54 C ATOM 936O LYS A 450 −12.829 −0.138 −2.926 1.00 23.77 O ATOM 937 N TYR A 451−11.093 −0.035 −4.339 1.00 22.16 N ATOM 938 CA TYR A 451 −11.490 −1.254−5.053 1.00 25.84 C ATOM 939 CB TYR A 451 −10.606 −1.466 −6.295 1.0030.33 C ATOM 940 CG TYR A 451 −10.851 −2.776 7.036 1.00 26.97 C ATOM 941CD1 TYR A 451 −11.957 −2.942 −7.887 1.00 32.31 C ATOM 942 CE1 TYR A 451−12.156 −4.161 −8.577 1.00 35.26 C ATOM 943 CD2 TYR A 451 −9.975 −3.841−6.887 1.00 29.55 C ATOM 944 CE2 TYR A 451 −10.171 −5.039 −7.538 1.0038.20 C ATOM 945 CZ TYR A 451 −11.250 −5.202 −8.384 1.00 34.79 C ATOM946 OH TYR A 451 −11.351 −6.416 −9.028 1.00 33.34 O ATOM 947 C TYR A 451−11.413 −2.477 −4.156 1.00 25.12 C ATOM 948 O TYR A 451 −12.349 −3.279−4.111 1.00 21.15 O ATOM 949 N LEU A 452 −10.317 −2.621 −3.411 1.0023.09 N ATOM 950 CA LEU A 452 −10.190 −3.769 −2.528 1.00 22.43 C ATOM951 CB LEU A 452 −8.812 −3.775 −1.805 1.00 24.62 C ATOM 952 CG LEU A 452−7.633 −4.080 −2.723 1.00 29.88 C ATOM 953 CD1 LEU A 452 −6.355 −3.885−1.901 1.00 40.57 C ATOM 954 CD2 LEU A 452 −7.706 −5.499 −3.261 1.0037.63 C ATOM 955 C LEU A 452 −11.289 −3.770 −1.487 1.00 23.29 C ATOM 956O LEU A 452 −11.835 −4.835 −1.160 1.00 24.20 O ATOM 957 N GLU A 453−11.615 −2.586 −0.966 1.00 21.59 N ATOM 958 CA GLU A 453 −12.644 −2.4650.044 1.00 23.71 C ATOM 959 CB GLU A 453 −12.707 −1.020 0.530 1.00 26.43C ATOM 960 CG GLU A 453 −13.831 −0.730 1.517 1.00 27.65 C ATOM 961 CDGLU A 453 −13.831 0.727 1.990 1.00 34.87 C ATOM 962 OE1 GLU A 453−14.451 1.582 1.298 1.00 33.02 O ATOM 963 OE2 GLU A 453 −13.200 1.0123.042 1.00 30.22 C ATOM 964 C GLU A 453 −14.014 −2.901 −0.520 1.00 27.31C ATOM 965 O GLU A 453 −14.763 −3.656 0.129 1.00 25.17 O ATOM 966 N GLUA 454 −14.348 −2.407 −1.706 1.00 22.10 N ATOM 967 CA GLU A 454 −15.640−2.769 −2.310 1.00 25.66 C ATOM 968 CB GLU A 454 −15.871 −1.997 −3.6191.00 31.24 C ATOM 969 CG GLU A 454 −14.964 −2.392 −4.754 1.00 42.57 CATOM 970 CD GLU A 454 −15.261 −1.624 −6.046 1.00 58.39 C ATOM 971 OE1GLU A 454 −15.273 −0.363 −6.015 1.00 51.95 O ATOM 972 OE2 GLU A 454−15.472 −2.287 −7.094 1.00 58.17 O ATOM 973 C GLU A 454 −15.721 −4.263−2.581 1.00 31.04 C ATOM 974 O GLU A 454 −16.810 −4.837 −2.583 1.0030.48 O ATOM 975 N LYS A 455 −14.583 −4.915 −2.799 1.00 24.65 N ATOM 976CA LYS A 455 −14.580 −6.358 −3.056 1.00 26.01 C ATOM 977 CB LYS A 455−13.474 6.742 −4.058 1.00 26.87 C ATOM 978 CG LYS A 455 −13.600 −6.047−5.435 1.00 32.48 C ATOM 979 CD LYS A 455 −14.919 −6.413 −6.093 1.0034.46 C ATOM 980 CE LYS A 455 −15.166 −5.643 −7.397 1.00 39.80 C ATOM981 NZ LYS A 455 −16.498 −6.028 −7.995 1.00 35.47 N ATOM 982 C LYS A 455−14.402 −7.158 −1.764 1.00 25.88 C ATOM 983 O LYS A 455 −14.205 −8.367−1.799 1.00 33.28 O ATOM 984 N ASN A 456 −14.484 −6.474 −0.632 1.0026.80 N ATOM 985 CA ASN A 456 −14.348 −7.110 0.679 1.00 33.33 C ATOM 986CB ASN A 456 −15.537 −8.042 0.956 1.00 33.66 C ATOM 987 CG ASN A 456−16.833 −7.293 1.019 1.00 41.21 C ATOM 988 OD1 ASN A 456 −17.005 −6.3971.847 1.00 38.41 O ATOM 989 ND2 ASN A 456 −17.763 −7.640 0.128 1.0043.69 N ATOM 990 C ASN A 456 −13.048 −7.865 0.932 1.00 32.96 C ATOM 991O ASN A 456 −13.065 −8.982 1.447 1.00 29.31 O ATOM 992 N PHE A 457−11.925 −7.265 0.539 1.00 25.61 N ATOM 993 CA PHE A 457 −10.633 −7.8710.827 1.00 23.17 C ATOM 994 CB PHE A 457 −9.823 −8.104 −0.457 1.00 24.54C ATOM 995 CG PHE A 457 −10.302 −9.259 −1.274 1.00 27.01 C ATOM 996 CD1PHE A 457 −11.141 −9.064 −2.372 1.00 38.40 C ATOM 997 CD2 PHE A 457−9.912 −10.546 −0.952 1.00 30.92 C ATOM 998 CE1 PHE A 457 −11.573−10.154 −3.131 1.00 40.99 C ATOM 999 CE2 PHE A 457 −10.338 −11.633−1.702 1.00 39.35 C ATOM 1000 CZ PHE A 457 −11.169 −11.435 −2.792 1.0032.26 C ATOM 1001 C PHE A 457 −9.876 −6.876 1.724 1.00 22.95 C ATOM 1002O PHE A 457 −10.006 −5.666 1.538 1.00 26.81 O ATOM 1003 N VAL A 458−9.095 −7.404 2.677 1.00 22.07 N ATOM 1004 CA VAL A 458 −8.271 −6.5873.574 1.00 18.40 C ATOM 1005 CB VAL A 458 −8.476 −6.999 5.067 1.00 24.28C ATOM 1006 CG1 VAL A 458 −7.490 −6.239 5.978 1.00 19.09 C ATOM 1007 CG2VAL A 458 −9.885 −6.680 5.496 1.00 24.91 C ATOM 1008 C VAL A 458 −6.811−6.870 3.172 1.00 21.95 C ATOM 1009 O VAL A 458 −6.412 −8.007 3.081 1.0022.78 O ATOM 1010 N HIS A 459 −6.017 −5.836 2.953 1.00 23.11 N ATOM 1011CA HIS A 459 −4.620 −6.058 2.514 1.00 22.90 C ATOM 1012 CB HIS A 459−4.106 −4.777 1.821 1.00 25.33 C ATOM 1013 CG HIS A 459 −2.735 −4.9151.233 1.00 27.05 C ATOM 1014 CD2 HIS A 459 −2.319 −4.984 −0.055 1.0035.51 C ATOM 1015 ND1 HIS A 459 −1.598 −4.995 2.004 1.00 30.45 N ATOM1016 CE1 HIS A 459 −0.539 −5.097 1.218 1.00 30.89 C ATOM 1017 NE2 HIS A459 −0.950 −5.091 −0.037 1.00 27.20 N ATOM 1018 C HIS A 459 −3.726−6.406 3.702 1.00 22.15 C ATOM 1019 O HIS A 459 −2.926 −7.373 3.669 1.0026.50 O ATOM 1020 N ARG A 460 −3.870 −5.592 4.743 1.00 22.61 N ATOM 1021CA ARG A 460 −3.160 −5.697 6.007 1.00 21.98 C ATOM 1022 CB ARG A 460−3.202 −7.138 6.526 1.00 27.77 C ATOM 1023 CG ARG A 460 −2.704 −7.2267.957 1.00 39.24 C ATOM 1024 CD ARG A 460 −2.722 −8.632 8.504 1.00 31.08C ATOM 1025 NE ARG A 460 −1.706 −8.745 9.539 1.00 33.21 N ATOM 1026 CZARG A 460 −1.459 −9.857 10.236 1.00 39.79 C ATOM 1027 NH1 ARG A 460−2.161 −10.955 10.014 1.00 32.10 N ATOM 1028 NH2 ARG A 460 −0.492 −9.86611.146 1.00 40.69 N ATOM 1029 C ARG A 460 −1.706 −5.211 6.022 1.00 28.94C ATOM 1030 O ARG A 460 −1.177 −4.874 7.079 1.00 36.64 O ATOM 1031 N ASPA 461 −1.072 −5.145 4.861 1.00 24.64 N ATOM 1032 CA ASP A 461 0.325−4.733 4.836 1.00 26.58 C ATOM 1033 CB ASP A 461 1.172 −5.943 4.374 1.0027.03 C ATOM 1034 CG ASP A 461 2.667 −5.827 4.743 1.00 38.59 C ATOM 1035OD1 ASP A 461 3.050 −4.953 5.551 1.00 48.65 O ATOM 1036 OD2 ASP A 4613.468 −6.646 4.224 1.00 49.76 O ATOM 1037 C ASP A 461 0.521 −3.500 3.9321.00 27.57 C ATOM 1038 O ASP A 461 1.524 −3.370 3.237 1.00 26.49 O ATOM1039 N LEU A 462 −0.429 −2.572 3.956 1.00 22.27 N ATOM 1040 CA LEU A 462−0.278 −1.380 3.139 1.00 21.53 C ATOM 1041 CB LEU A 462 −1.636 −0.6662.987 1.00 22.43 C ATOM 1042 CG LEU A 462 −1.648 0.602 2.128 1.00 30.85C ATOM 1043 CD1 LEU A 462 −1.215 0.224 0.715 1.00 29.37 C ATOM 1044 CD2LEU A 462 −3.042 1.270 2.133 1.00 27.57 C ATOM 1045 C LEU A 462 0.779−0.477 3.804 1.00 22.66 C ATOM 1046 O LEU A 462 0.671 −0.125 4.950 1.0026.45 O ATOM 1047 N ALA A 463 1.832 −0.159 3.063 1.00 21.02 N ATOM 1048CA ALA A 463 2.926 0.688 3.572 1.00 19.38 C ATOM 1049 CB ALA A 463 3.865−0.138 4.481 1.00 20.15 C ATOM 1050 C ALA A 463 3.669 1.169 2.323 1.0017.38 C ATOM 1051 O ALA A 463 3.586 0.534 1.274 1.00 21.49 O ATOM 1052 NALA A 464 4.383 2.277 2.438 1.00 20.81 N ATOM 1053 CA ALA A 464 5.0622.797 1.271 1.00 22.24 C ATOM 1054 CB ALA A 464 5.810 4.094 1.651 1.0019.74 C ATOM 1055 C ALA A 464 6.005 1.777 0.641 1.00 23.62 C ATOM 1056 OALA A 464 6.180 1.782 −0.571 1.00 22.85 O ATOM 1057 N ARG A 465 6.6110.915 1.457 1.00 23.55 N ATOM 1058 CA ARG A 465 7.528 −0.112 0.962 1.0022.78 C ATOM 1059 CB ARG A 465 8.203 −0.852 2.133 1.00 26.22 C ATOM 1060CG ARG A 465 7.254 −1.662 3.026 1.00 22.40 C ATOM 1061 CD ARG A 4657.980 −2.238 4.272 1.00 27.73 C ATOM 1062 NE ARG A 465 7.030 −2.8735.180 1.00 32.59 N ATOM 1063 CZ ARG A 465 6.337 −2.232 6.126 1.00 41.47C ATOM 1064 NH1 ARG A 465 6.491 −0.928 6.320 1.00 34.18 N ATOM 1065 NH2ARG A 465 5.441 −2.887 6.841 1.00 40.07 N ATOM 1066 C ARG A 465 6.814−1.136 0.084 1.00 24.95 C ATOM 1067 O ARG A 465 7.461 −1.867 −0.673 1.0025.58 O ATOM 1068 N ASN A 466 5.484 −1.203 0.199 1.00 24.98 N ATOM 1069CA ASN A 466 4.715 −2.149 −0.603 1.00 23.15 C ATOM 1070 CB ASN A 4663.785 −2.982 0.276 1.00 20.54 C ATOM 1071 CG ASN A 466 4.537 −3.9871.118 1.00 29.73 C ATOM 1072 OD1 ASN A 466 5.600 −4.469 0.710 1.00 26.55O ATOM 1073 ND2 ASN A 466 4.000 −4.310 2.302 1.00 25.54 N ATOM 1074 CASN A 466 3.947 −1.509 −1.752 1.00 23.75 C ATOM 1075 O ASN A 466 3.185−2.171 −2.422 1.00 24.79 O ATOM 1076 N VAL A 467 4.170 −0.220 −1.9591.00 21.31 N ATOM 1077 CA VAL A 467 3.561 0.462 −3.086 1.00 19.34 C ATOM1078 CB VAL A 467 3.127 1.872 −2.699 1.00 21.47 C ATOM 1079 CG1 VAL A467 2.736 2.647 −3.979 1.00 22.29 C ATOM 1080 CG2 VAL A 467 1.957 1.792−1.696 1.00 19.95 C ATOM 1081 C VAL A 467 4.733 0.538 −4.076 1.00 22.01C ATOM 1082 O VAL A 467 5.817 1.025 3.721 1.00 22.82 O ATOM 1083 N LEU A468 4.524 0.036 −5.290 1.00 21.63 N ATOM 1084 CA LEU A 468 5.601 0.021−6.286 1.00 25.97 C ATOM 1085 CB LEU A 468 5.828 −1.399 −6.801 1.0021.35 C ATOM 1086 CG LEU A 468 6.073 −2.498 −5.767 1.00 25.31 C ATOM1087 CD1 LEU A 468 5.995 −3.859 −6.430 1.00 25.16 C ATOM 1088 CD2 LEU A468 7.434 −2.267 −5.110 1.00 27.20 C ATOM 1089 C LEU A 468 5.285 0.920−7.465 1.00 29.27 C ATOM 1090 O LEU A 468 4.143 1.006 −7.884 1.00 26.29O ATOM 1091 N LEU A 469 6.311 1.554 −8.035 1.00 24.41 N ATOM 1093 CA LEUA 469 6.063 2.440 −9.156 1.00 25.24 C ATOM 1093 CB LEU A 469 6.886 3.714−8.973 1.00 28.20 C ATOM 1094 CG LEU A 469 6.583 4.441 −7.661 1.00 40.39C ATOM 1095 CD1 LEU A 469 7.566 5.547 −7.471 1.00 42.75 C ATOM 1096 CD2LEU A 469 5.180 5.007 −7.681 1.00 36.92 C ATOM 1097 C LEU A 469 6.3561.844 −10.518 1.00 25.99 C ATOM 1098 O LEU A 469 7.411 1.237 −10.7291.00 27.91 O ATOM 1099 N VAL A 470 5.416 1.985 −11.445 1.00 27.37 N ATOM1100 CA VAL A 470 5.662 1.526 −12.795 1.00 27.70 C ATOM 1101 CB VAL A470 4.369 1.352 −13.589 1.00 30.57 C ATOM 1102 CG1 VAL A 470 4.693 1.012−15.042 1.00 35.99 C ATOM 1103 CG2 VAL A 470 3.536 0.219 −12.963 1.0028.74 C ATOM 1104 C VAL A 470 6.517 2.663 −13.384 1.00 32.73 C ATOM 1105O VAL A 470 7.467 2.415 −14.137 1.00 35.56 O ATOM 1106 N ASN A 471 6.1723.895 −13.012 1.00 30.15 N ATOM 1107 CA ASN A 471 6.889 5.122 −13.4151.00 35.49 C ATOM 1108 CB ASN A 471 6.441 5.610 −14.805 1.00 38.79 CATOM 1109 CG ASN A 471 4.941 5.766 −14.912 1.00 38.59 C ATOM 1110 OD1ASN A 471 4.246 4.841 −15.320 1.00 61.19 O ATOM 1111 ND2 ASN A 471 4.4326.917 −14.518 1.00 37.18 N ATOM 1112 C ASN A 471 6.561 6.186 −12.3661.00 34.10 C ATOM 1113 O ASN A 471 5.766 5.925 −11.458 1.00 31.54 O ATOM1114 N ARG A 472 7.144 7.383 −12.468 1.00 31.44 N ATOM 1115 CA ARG A 4726.889 8.423 −11.467 1.00 34.23 C ATOM 1116 CB ARG A 472 7.812 9.628−11.699 1.00 36.29 C ATOM 1117 CG ARG A 472 7.539 10.352 −13.002 1.0038.64 C ATOM 1118 CD ARG A 472 8.440 11.577 −13.126 1.00 42.01 C ATOM1119 NE ARG A 472 7.960 12.686 −12.310 1.00 42.62 N ATOM 1120 CZ ARG A472 8.611 13.835 −12.142 1.00 49.56 C ATOM 1121 NH1 ARG A 472 9.78914.036 −12.734 1.00 41.21 N ATOM 1122 NH2 ARG A 472 8.082 14.791 −11.3951.00 45.67 N ATOM 1123 C ARG A 472 5.442 8.907 −11.393 1.00 23.39 C ATOM1124 O ARG A 472 5.087 9.644 −10.491 1.00 29.27 O ATOM 1125 N HIS A 4734.621 8.504 −12.357 1.00 26.03 N ATOM 1126 CA HIS A 473 3.234 8.911−12.392 1.00 32.63 C ATOM 1127 CB HIS A 473 2.947 9.729 −13.680 1.0027.76 C ATOM 1128 CG HIS A 473 3.693 11.026 −13.743 1.00 31.49 C ATOM1129 CD1 HIS A 473 4.728 11.426 −14.522 1.00 40.44 C ATOM 1130 ND1 HIS A473 3.462 12.056 −12.858 1.00 33.49 N ATOM 1131 CE1 HIS A 473 4.32713.031 −13.082 1.00 42.59 C ATOM 1132 NE2 HIS A 473 5.108 12.673 −14.0861.00 41.30 N ATOM 1133 C HIS A 473 2.296 7.710 −12.329 1.00 28.13 C ATOM1134 O HIS A 473 1.105 7.842 −12.651 1.00 25.55 O ATOM 1135 N TYR A 4742.813 6.547 −11.928 1.00 26.97 N ATOM 1136 CA TYR A 474 1.957 5.357−11.889 1.00 29.51 C ATOM 1137 CB TYR A 474 1.991 4.652 −13.250 1.0026.22 C ATOM 1138 CG TYR A 474 0.982 3.515 −13.472 1.00 30.97 C ATOM1139 CD1 TYR A 474 −0.077 3.274 −12.582 1.00 28.77 C ATOM 1140 CE1 TYR A474 −1.001 −2.218 −12.823 1.00 31.08 C ATOM 1141 CD2 TYR A 474 1.0912.689 −14.596 1.00 33.81 C ATOM 1142 CE2 TYR A 474 0.191 1.658 −14.8381.00 34.98 C ATOM 1143 CZ TYR A 474 −0.853 1.418 −13.960 1.00 33.21 CATOM 1144 OH TYR A 474 −1.723 0.375 −14.256 1.00 31.45 O ATOM 1145 C TYRA 474 2.358 4.376 −10.789 1.00 25.47 C ATOM 1146 O TYR A 474 3.336 3.636−10.932 1.00 28.97 O ATOM 1147 N ALA A 475 1.571 4.374 −9.710 1.00 22.78N ATOM 1148 CA ALA A 475 1.837 3.495 −8.577 1.00 26.62 C ATOM 1149 CBALA A 475 1.696 4.297 −7.265 1.00 27.18 C ATOM 1150 C ALA A 475 0.8972.280 −8.553 1.00 28.20 C ATOM 1151 O ALA A 475 −0.234 2.341 −9.045 1.0025.92 O ATOM 1152 N LYS A 476 1.380 1.169 −7.990 1.00 24.41 N ATOM 1153CA LYS A 476 0.569 −0.039 −7.855 1.00 23.63 C ATOM 1154 CB LYS A 4760.957 −1.092 −8.912 1.00 26.51 C ATOM 1155 CG LYS A 476 0.418 −0.795−10.305 1.00 27.53 C ATOM 1156 CD LYS A 476 0.985 −1.811 −11.310 1.0032.34 C ATOM 1157 CE LYS A 476 0.273 −1.748 −12.657 1.00 36.56 C ATOM1158 NZ LYS A 476 −0.989 −2.542 −12.605 1.00 37.90 N ATOM 1159 C LYS A476 0.772 −0.657 −6.477 1.00 25.52 C ATOM 1160 O LYS A 476 1.898 −0.684−5.956 1.00 25.22 O ATOM 1161 N ILE A 477 −0.309 −1.172 −5.896 1.0022.11 N ATOM 1162 CA ILE A 477 −0.214 −1.800 −4.580 1.00 24.01 C ATOM1163 CB ILE A 477 −1.577 −1.846 −3.915 1.00 21.78 C ATOM 1164 CG2 ILE A477 −1.499 −2.642 −2.596 1.00 25.26 C ATOM 1165 CG1 ILE A 477 −2.081−0.417 −3.708 1.00 20.73 C ATOM 1166 CD1 ILE A 477 −3.578 −0.332 −3.5341.00 22.58 C ATOM 1167 C ILE A 477 0.267 −3.223 −4.766 1.00 24.46 C ATOM1168 O ILE A 477 −0.216 −3.919 −5.654 1.00 22.86 O ATOM 1169 N SER A 4781.214 −3.666 −3.932 1.00 22.32 N ATOM 1170 CA SER A 478 1.691 −5.039−4.071 1.00 22.20 C ATOM 1171 CB SER A 478 3.097 −5.049 −4.649 1.0028.05 C ATOM 1172 OG SER A 478 3.965 −4.509 −3.674 1.00 38.71 O ATOM1173 C SER A 478 1.723 −5.787 −2.738 1.00 26.29 C ATOM 1174 O SER A 4781.311 −5.261 −1.697 1.00 25.87 O ATOM 1175 N ASP A 479 2.247 −7.010−2.810 1.00 23.81 N ATOM 1176 CA ASP A 479 2.394 −7.959 −1.690 1.0025.45 C ATOM 1177 CB ASP A 479 3.465 −7.519 −0.666 1.00 24.64 C ATOM1178 CG ASP A 479 3.850 −8.767 0.288 1.00 35.61 C ATOM 1179 OD1 ASP A479 3.141 −9.710 0.289 1.00 30.47 O ATOM 1180 OD2 ASP A 479 4.860 −8.5671.018 1.00 31.61 O ATOM 1181 C ASP A 479 1.099 −8.294 −0.952 1.00 21.75C ATOM 1182 O ASP A 479 0.819 −7.751 0.144 1.00 21.47 O ATOM 1183 N PHEA 480 0.359 −9.246 −1.524 1.00 24.40 N ATOM 1184 CA PHE A 480 −0.905−9.719 −0.946 1.00 27.55 C ATOM 1185 CB PHE A 480 −1.910 −9.973 −2.0771.00 22.84 C ATOM 1186 CG PHE A 480 −2.335 −8.709 −2.776 1.00 25.54 CATOM 1187 CD1 PHE A 480 −3.472 −7.999 −2.373 1.00 37.22 C ATOM 1188 CD2PHE A 480 −1.531 −8.165 −3.774 1.00 29.75 C ATOM 1189 CE1 PHE A 480−3.788 6.767 −2.950 1.00 36.53 C ATOM 1190 CE2 PHE A 480 −1.841 −6.925−4.351 1.00 31.15 C ATOM 1191 CZ PHE A 480 −2.956 −6.229 −3.945 1.0030.92 C ATOM 1192 C PHE A 480 −0.734 −10.978 −0.070 1.00 22.25 C ATOM1193 O PHE A 480 −1.693 −11.697 0.201 1.00 28.80 O ATOM 1194 N GLY A 4810.494 −11.200 0.395 1.00 26.68 N ATOM 1195 CA GLY A 481 0.808 −12.3541.234 1.00 25.28 C ATOM 1196 C GLY A 481 0.041 −12.422 2.553 1.00 29.85C ATOM 1197 O GLY A 481 −0.094 −13.489 3.125 1.00 28.84 O ATOM 1198 NLEU A 482 −0.455 −11.293 3.049 1.00 21.56 N ATOM 1199 CA LEU A 482−1.217 −11.299 4.316 1.00 23.95 C ATOM 1200 CB LEU A 482 −0.608 −10.2875.304 1.00 25.94 C ATOM 1201 CG LEU A 482 0.789 −10.660 5.792 1.00 31.12C ATOM 1202 CD1 LEU A 482 1.418 −9.482 6.554 1.00 34.67 C ATOM 1203 CD2LEU A 482 0.680 −11.884 6.675 1.00 35.08 C ATOM 1204 C LEU A 482 −2.667−10.925 4.097 1.00 21.10 C ATOM 1205 O LEU A 482 −3.441 −10.766 5.0501.00 26.73 O ATOM 1206 N SER A 483 −3.050 −10.794 2.837 1.00 21.83 NATOM 1207 CA SER A 483 −4.409 −10.375 2.518 1.00 17.76 C ATOM 1208 CBSER A 483 −4.465 −9.958 1.042 1.00 22.28 C ATOM 1209 OG SER A 483 −3.595−8.851 0.860 1.00 29.25 O ATOM 1210 C SER A 483 −5.440 −11.475 2.7851.00 21.06 C ATOM 1211 O SER A 483 −5.128 −12.645 2.739 1.00 24.20 OATOM 1212 N LYS A 484 −6.681 −11.071 3.034 1.00 20.71 N ATOM 1213 CA LYSA 484 −7.738 −12.041 3.291 1.00 21.00 C ATOM 1214 CB LYS A 484 −7.862−12.318 4.791 1.00 24.78 C ATOM 1215 CG LYS A 484 −6.650 −13.105 5.3621.00 38.83 C ATOM 1216 CD LYS A 484 −6.770 −13.393 6.859 1.00 45.27 CATOM 1217 CE LYS A 484 −5.677 −14.378 7.302 1.00 43.33 C ATOM 1218 NZLYS A 484 −4.326 −14.049 6.778 1.00 56.25 N ATOM 1219 C LYS A 484 −9.076−11.545 2.768 1.00 25.54 C ATOM 1220 O LYS A 484 −9.320 −10.348 2.6771.00 26.31 O ATOM 1221 N ALA A 485 −9.941 −12.491 2.434 1.00 23.65 NATOM 1222 CA ALA A 485 −11.280 −12.138 1.974 1.00 22.67 C ATOM 1223 CBALA A 485 −11.814 −13.210 0.995 1.00 31.69 C ATOM 1224 C ALA A 485−12.144 −12.086 3.249 1.00 31.19 C ATOM 1225 O ALA A 485 −12.006 −12.9314.136 1.00 29.37 O ATOM 1226 N LEU A 486 −12.995 −11.073 3.349 1.0023.82 N ATOM 1227 CA LEU A 486 −13.873 −10.926 4.518 1.00 20.69 C ATOM1228 CB LEU A 486 −14.113 −9.435 4.825 1.00 28.46 C ATOM 1229 CG LEU A486 −13.031 −8.604 5.532 1.00 31.01 C ATOM 1230 CD1 LEU A 486 −13.418−7.137 5.591 1.00 36.09 C ATOM 1231 CD2 LEU A 486 −12.840 −9.129 6.9231.00 37.43 C ATOM 1232 C LEU A 486 −15.239 −11.583 4.288 1.00 31.06 CATOM 1233 O LEU A 486 −15.911 −11.953 5.235 1.00 33.37 O ATOM 1234 N GLYA 487 −15.651 −11.715 3.031 1.00 28.59 N ATOM 1235 CA GLY A 487 −16.955−12.284 2.753 1.00 33.58 C ATOM 1236 C GLY A 487 −18.031 −11.345 3.2831.00 38.11 C ATOM 1237 O GLY A 487 −17.980 −10.144 3.077 1.00 36.30 OATOM 1238 N ALA A 488 −18.987 −11.910 4.004 1.00 38.66 N ATOM 1239 CAALA A 488 −20.092 −11.130 4.556 1.00 40.22 C ATOM 1240 CB ALA A 488−21.287 −12.045 4.812 1.00 46.29 C ATOM 1241 C ALA A 488 −19.733 −10.3885.843 1.00 40.58 C ATOM 1242 O ALA A 488 −20.438 −9.532 6.295 1.00 40.10O ATOM 1243 N ASP A 489 −18.578 −10.699 6.422 1.00 36.35 N ATOM 1244 CAASP A 489 −18.160 −10.041 7.672 1.00 35.41 C ATOM 1245 CB ASP A 489−17.192 −10.955 8.431 1.00 37.29 C ATOM 1246 CG ASP A 489 −17.782−12.314 8.686 1.00 49.00 C ATOM 1247 OD1 ASP A 489 −19.013 −12.383 8.9091.00 49.08 O ATOM 1248 OD2 ASP A 489 −17.018 −13.305 8.680 1.00 50.85 OATOM 1249 C ASP A 489 −17.508 −8.676 7.484 1.00 30.55 C ATOM 1250 O ASPA 489 −16.974 −8.388 6.427 1.00 32.36 O ATOM 1251 N ASP A 490 −17.538−7.845 8.529 1.00 28.02 N ATOM 1252 CA ASP A 490 −16.923 −6.527 8.4411.00 31.41 C ATOM 1253 CB ASP A 490 −17.768 −5.486 9.178 1.00 38.68 CATOM 1254 CG ASP A 490 −17.934 −5.812 10.630 1.00 48.46 C ATOM 1255 OD1ASP A 490 −18.996 −5.471 11.213 1.00 57.52 O ATOM 1256 OD2 ASP A 490−16.999 −6.397 11.198 1.00 54.69 O ATOM 1257 C ASP A 490 −15.492 −6.5238.983 1.00 26.85 C ATOM 1258 O ASP A 490 −14.799 −5.512 8.906 1.00 24.78O ATOM 1259 N SER A 491 −15.046 −7.652 9.521 1.00 23.91 N ATOM 1260 CASER A 491 −13.666 −7.760 10.031 1.00 22.38 C ATOM 1261 CB SER A 491−13.522 −6.993 11.336 1.00 29.00 C ATOM 1262 OG SER A 491 −14.280 −7.63412.371 1.00 32.97 O ATOM 1263 C SER A 491 −13.333 −9.202 10.309 1.0029.41 C ATOM 1264 O SER A 491 −14.204 −10.076 10.200 1.00 25.81 O ATOM1265 N TYR A 492 −12.068 −9.462 10.640 1.00 23.00 N ATOM 1266 CA TYR A492 −11.679 −10.788 11.033 1.00 26.00 C ATOM 1267 CB TYR A 492 −11.165−11.647 9.858 1.00 26.94 C ATOM 1268 CG TYR A 492 −9.811 −11.265 9.3281.00 26.14 C ATOM 1269 CD1 TYR A 492 −8.639 −11.830 9.855 1.00 24.16 CATOM 1270 CE1 TYR A 492 −7.378 −11.414 9.419 1.00 28.54 C ATOM 1271 CD2TYR A 492 −9.693 −10.285 8.348 1.00 25.38 C ATOM 1272 CE2 TYR A 492−8.424 −9.859 7.902 1.00 23.56 C ATOM 1273 CZ TYR A 492 −7.282 −10.4288.447 1.00 26.57 C ATOM 1274 OH TYR A 492 −6.040 −9.993 8.045 1.00 24.90O ATOM 1275 C TYR A 492 −10.630 −10.613 12.122 1.00 23.17 C ATOM 1276 OTYR A 492 −10.082 −9.521 12.308 1.00 22.18 O ATOM 1277 N TYR A 493−10.404 −11.690 12.865 1.00 21.40 N ATOM 1278 CA TYR A 493 −9.406−11.705 13.943 1.00 18.61 C ATOM 1279 CB TYR A 493 −10.015 −12.16815.262 1.00 23.77 C ATOM 1280 CG TYR A 493 −10.965 −11.174 15.837 1.0024.82 C ATOM 1281 CD1 TYR A 493 −12.229 −11.002 15.282 1.00 26.28 C ATOM1282 CE1 TYR A 493 −13.105 −10.061 15.789 1.00 33.92 C ATOM 1283 CD2 TYRA 493 −10.598 −10.375 16.921 1.00 24.00 C ATOM 1284 CE2 TYR A 493−11.468 −9.431 17.439 1.00 29.62 C ATOM 1285 CZ TYR A 493 −12.719 −9.28416.868 1.00 33.02 C ATOM 1286 OH TYR A 493 −13.592 −8.384 17.410 1.0032.06 O ATOM 1287 C TYR A 493 −8.394 −12.708 13.459 1.00 19.01 C ATOM1288 O TYR A 493 −8.749 −13.842 13.091 1.00 22.83 O ATOM 1289 N THR A494 −7.141 −12.272 13.400 1.00 26.38 N ATOM 1290 CA THR A 494 −6.077−13.079 12.834 1.00 32.64 C ATOM 1291 CB THR A 494 −5.029 −12.172 12.1191.00 31.23 C ATOM 1292 OG1 THR A 494 −4.099 −12.987 11.401 1.00 41.68 OATOM 1293 OG2 THR A 494 −4.270 −11.355 13.123 1.00 33.57 C ATOM 1294 CTHR A 494 −5.332 −13.934 13.830 1.00 34.49 C ATOM 1295 O THR A 494−5.210 −13.605 15.005 1.00 28.24 O ATOM 1296 N ALA A 495 −4.747 −15.00613.322 1.00 44.02 N ATOM 1297 CA ALA A 495 −3.959 −15.870 14.166 1.0044.59 C ATOM 1298 CB ALA A 495 −3.887 −17.248 13.552 1.00 46.73 C ATOM1299 C ALA A 495 −2.562 −15.276 14.307 1.00 50.58 C ATOM 1300 O ALA A495 −2.108 −14.536 13.439 1.00 49.05 O ATOM 1301 N ARG A 496 −1.899−15.593 15.409 1.00 54.28 N ATOM 1302 CA ARG A 496 −0.552 −15.110 15.6681.00 58.65 C ATOM 1303 CB ARG A 496 −0.261 −15.109 17.173 1.00 60.21 CATOM 1304 CG ARG A 496 0.432 −13.854 17.698 1.00 65.46 C ATOM 1305 CDARG A 496 1.644 −13.487 16.885 1.00 66.41 C ATOM 1306 NE ARG A 496 2.227−12.233 17.353 1.00 67.01 N ATOM 1307 CZ ARG A 496 3.254 −11.624 16.7711.00 70.08 C ATOM 1308 NH1 ARG A 496 3.816 −12.156 15.690 1.00 71.57 NATOM 1309 NH2 ARG A 496 3.722 −10.486 17.268 1.00 67.36 N ATOM 1310 CARG A 496 0.441 −16.048 14.971 1.00 60.54 C ATOM 1311 O ARG A 496 0.365−17.270 15.112 1.00 59.09 O ATOM 1312 N SER A 497 1.362 −15.475 14.2091.00 58.17 N ATOM 1313 CA SER A 497 2.370 −16.275 13.523 1.00 60.35 CATOM 1314 CB SER A 497 2.276 −16.074 12.010 1.00 60.39 C ATOM 1315 OGSER A 497 2.664 −14.760 11.653 1.00 64.92 O ATOM 1316 C SER A 497 3.736−15.821 14.016 1.00 60.92 C ATOM 1317 O SER A 497 3.836 −14.890 14.8171.00 58.88 O ATOM 1318 N ALA A 498 4.781 −16.480 13.531 1.00 63.41 NATOM 1319 CA ALA A 498 6.146 −16.143 13.911 1.00 61.88 C ATOM 1320 CBALA A 498 7.102 −17.263 13.482 1.00 59.84 C ATOM 1321 C ALA A 498 6.556−14.827 13.254 1.00 60.58 C ATOM 1322 O ALA A 498 6.132 −14.515 12.1381.00 60.40 O ATOM 1323 N GLY A 499 7.381 −14.057 13.950 1.00 60.46 NATOM 1324 CA GLY A 499 7.833 −12.798 13.393 1.00 63.38 C ATOM 1325 C GLYA 499 7.226 −11.608 14.100 1.00 61.34 C ATOM 1326 O GLY A 499 6.240−11.741 14.827 1.00 64.30 O ATOM 1327 N LYS A 500 7.817 −10.440 13.8861.00 60.00 N ATOM 1328 CA LYS A 500 7.338 −9.216 14.511 1.00 56.90 CATOM 1329 CB LYS A 500 8.502 −8.246 14.717 1.00 60.17 C ATOM 1330 CG LYSA 500 9.535 −8.705 15.729 1.00 63.00 C ATOM 1331 CD LYS A 500 8.991−8.599 17.148 1.00 67.02 C ATOM 1332 CE LYS A 500 10.049 −8.992 18.1741.00 65.56 C ATOM 1333 NZ LYS A 500 9.537 −8.897 19.573 1.00 68.82 NATOM 1334 C LYS A 500 6.272 −8.539 13.654 1.00 51.76 C ATOM 1335 O LYS A500 6.271 −8.656 12.434 1.00 48.14 O ATOM 1336 N TRP A 501 5.363 −7.82914.311 1.00 47.51 N ATOM 1337 CA TRP A 501 4.307 −7.104 13.602 1.0046.32 C ATOM 1338 CB TRP A 501 3.028 −7.109 14.441 1.00 41.88 C ATOM1339 CG TRP A 501 2.225 −8.356 14.335 1.00 37.72 C ATOM 1340 CD2 TRP A501 0.855 −8.518 14.721 1.00 36.73 C ATOM 1341 CE2 TRP A 501 0.471−9.832 14.363 1.00 39.69 C ATOM 1342 CE3 TRP A 501 −0.089 −7.679 15.3341.00 38.48 C ATOM 1343 CD1 TRP A 501 2.613 −9.547 13.789 1.00 42.00 CATOM 1344 NE1 TRP A 501 1.562 −10.441 13.797 1.00 38.68 N ATOM 1345 CZ2TRP A 501 −0.821 −10.325 14.593 1.00 35.30 C ATOM 1346 CZ3 TRP A 501−1.379 −8.176 15.565 1.00 32.86 C ATOM 1347 CH2 TRP A 501 −1.726 −9.48315.192 1.00 35.05 C ATOM 1348 C TRP A 501 4.765 −5.658 13.385 1.00 39.20C ATOM 1349 O TRP A 501 5.361 −5.063 14.279 1.00 42.54 O ATOM 1350 N PROA 502 4.500 −5.079 12.197 1.00 36.57 N ATOM 1351 CD PRO A 502 3.828−5.725 11.050 1.00 35.66 C ATOM 1352 CA PRO A 502 4.885 −3.689 11.8761.00 38.88 C ATOM 1353 CB PRO A 502 4.721 −3.623 10.359 1.00 37.46 CATOM 1354 CG PRO A 502 3.547 −4.559 10.117 1.00 42.86 C ATOM 1355 C PROA 502 3.908 −2.772 12.604 1.00 36.51 C ATOM 1356 O PRO A 502 3.018−2.152 11.988 1.00 28.01 O ATOM 1357 N LEU A 503 4.079 −2.706 13.9211.00 29.24 N ATOM 1358 CA LEU A 503 3.185 −1.931 14.780 1.00 29.71 CATOM 1359 CB LEU A 503 3.701 −1.950 16.227 1.00 36.06 C ATOM 1360 CG LEUA 503 3.999 −3.328 16.817 1.00 39.54 C ATOM 1361 CD1 LEU A 503 4.596−3.172 18.215 1.00 48.04 C ATOM 1362 CD2 LEU A 503 2.727 −4.145 16.8721.00 43.63 C ATOM 1363 C LEU A 503 2.962 −0.489 14.364 1.00 25.89 C ATOM1364 O LEU A 503 1.875 0.057 14.580 1.00 24.95 O ATOM 1365 N LYS A 5043.979 0.132 13.766 1.00 24.94 N ATOM 1366 CA LYS A 504 3.860 1.52713.379 1.00 25.26 C ATOM 1367 CB LYS A 504 5.223 2.090 12.978 1.00 28.02C ATOM 1368 CG LYS A 504 6.170 2.228 14.194 1.00 31.43 C ATOM 1369 CDLYS A 504 7.500 2.881 13.813 1.00 31.17 C ATOM 1370 CE LYS A 504 8.4472.979 15.011 1.00 36.32 C ATOM 1371 NZ LYS A 504 9.635 3.805 14.649 1.0038.54 N ATOM 1372 C LYS A 504 2.846 1.772 12.264 1.00 26.30 C ATOM 1373O LYS A 504 2.453 2.892 12.040 1.00 22.29 O ATOM 1374 N TRP A 505 2.4300.719 11.581 1.00 22.68 N ATOM 1375 CA TRP A 505 1.437 0.866 10.515 1.0018.95 C ATOM 1376 CB TRP A 505 1.890 0.096 9.275 1.00 25.33 C ATOM 1377CG TRP A 505 2.892 0.834 8.461 1.00 25.92 C ATOM 1378 CD2 TRP A 5054.295 0.938 8.717 1.00 24.46 C ATOM 1379 CE2 TRP A 505 4.834 1.808 7.7391.00 23.54 C ATOM 1380 CE3 TRP A 505 5.155 0.393 9.681 1.00 26.35 C ATOM1381 CD1 TRP A 505 2.633 1.615 7.365 1.00 19.83 C ATOM 1382 NE1 TRP A505 3.801 2.208 6.926 1.00 24.61 N ATOM 1383 CZ2 TRP A 505 6.198 2.1387.692 1.00 27.89 C ATOM 1384 CZ3 TRP A 505 6.516 0.709 9.635 1.00 27.25C ATOM 1385 CH2 TRP A 505 7.024 1.581 8.642 1.00 26.23 C ATOM 1386 C TRPA 505 0.070 0.305 10.971 1.00 22.11 C ATOM 1387 O TRP A 505 −0.926 0.42910.258 1.00 22.39 O ATOM 1388 N TYR A 506 0.027 −0.266 12.167 1.00 21.52N ATOM 1389 CA TYR A 506 −1.231 −0.889 12.650 1.00 22.86 C ATOM 1390 CBTYR A 506 −0.859 −2.165 13.422 1.00 21.24 C ATOM 1391 CG TYR A 506−0.540 −3.393 12.593 1.00 23.75 C ATOM 1392 CD1 TYR A 506 −0.335 −3.29711.221 1.00 25.21 C ATOM 1393 CE1 TYR A 506 −0.008 −4.434 10.444 1.0033.36 C ATOM 1394 CD2 TYR A 506 −0.424 −4.659 13.184 1.00 30.33 C ATOM1395 CE2 TYR A 506 −0.113 −5.795 12.413 1.00 33.98 C ATOM 1396 CZ TYR A506 0.100 −5.674 11.053 1.00 34.14 C ATOM 1397 OH TYR A 506 0.459 −6.78410.310 1.00 36.03 O ATOM 1398 C TYR A 506 −2.184 −0.017 13.500 1.0025.61 C ATOM 1399 O TYR A 506 −1.737 0.682 14.412 1.00 24.59 O ATOM 1400N ALA A 507 −3.490 −0.076 13.209 1.00 21.31 N ATOM 1401 CA ALA A 507−4.511 0.664 13.950 1.00 21.80 C ATOM 1402 CB ALA A 507 −5.894 0.50213.254 1.00 18.75 C ATOM 1403 C ALA A 507 −4.570 0.070 15.374 1.00 26.17C ATOM 1404 O ALA A 507 −4.161 −1.064 15.607 1.00 22.46 O ATOM 1405 NPRO A 508 −5.107 0.831 16.332 1.00 22.10 N ATOM 1406 CD PRO A 508 −5.5962.214 16.186 1.00 22.87 C ATOM 1407 CA PRO A 508 −5.213 0.370 17.7221.00 24.97 C ATOM 1408 CB PRO A 508 −5.979 1.499 18.403 1.00 25.74 CATOM 1409 CG PRO A 508 −5.555 2.711 17.600 1.00 34.90 C ATOM 1410 C PROA 508 −5.898 −0.978 17.600 1.00 28.04 C ATOM 1411 O PRO A 508 −5.3979−1.819 18.682 1.00 24.23 O ATOM 1412 N GLU A 509 −7.019 −1.193 17.2291.00 24.59 N ATOM 1413 CA GLU A 509 −7.754 −2.445 17.352 1.00 27.89 CATOM 1414 CB GLU A 509 −9.128 −2.368 16.654 1.00 27.01 C ATOM 1415 CGGLU A 509 −9.060 −2.329 15.121 1.00 23.52 C ATOM 1416 CD GLU A 509−8.971 −0.909 14.578 1.00 30.32 C ATOM 1417 OE1 GLU A 509 −8.712 0.03815.366 1.00 23.83 O ATOM 1418 OE2 GLU A 509 −9.139 −0.750 13.346 1.0024.89 O ATOM 1419 C GLU A 509 −6.954 −3.636 16.829 1.00 24.33 C ATOM1420 O GLU A 509 −7.196 −4.767 17.246 1.00 24.26 O ATOM 1421 N CYS A 510−6.009 −3.391 15.913 1.00 20.72 N ATOM 1422 CA CYS A 510 −5.173 −4.45615.392 1.00 18.85 C ATOM 1423 CB CYS A 510 −4.314 −3.963 14.213 1.0020.67 C ATOM 1424 SG CYS A 510 −5.287 −3.330 12.822 1.00 25.10 S ATOM1425 C CYS A 510 −4.216 −4.926 16.503 1.00 21.45 C ATOM 1426 O CYS A 510−4.026 −6.104 16.720 1.00 24.61 O ATOM 1427 N ILE A 511 −3.590 −3.97217.164 1.00 22.33 N ATOM 1428 CA ILE A 511 −2.629 −4.304 18.208 1.0027.31 C ATOM 1429 CB ILE A 511 −1.724 −3.081 18.537 1.00 27.85 C ATOM1430 CG2 ILE A 511 −0.701 −3.081 18.537 1.00 27.85 C ATOM 1431 CG1 ILE A511 −1.004 −2.638 17.255 1.00 27.31 C ATOM 1432 CD1 ILE A 511 −0.335−1.270 17.338 1.00 34.56 C ATOM 1433 C ILE A 511 −3.318 −4.797 19.4751.00 31.42 C ATOM 1434 O ILE A 511 −2.887 −5.791 20.071 1.00 29.83 OATOM 1435 N ASN A 512 −4.413 −4.152 19.861 1.00 24.92 N ATOM 1436 CA ASNA 512 −5.068 −4.547 21.093 1.00 27.73 C ATOM 1437 CB ASN A 512 −5.860−3.387 21.681 1.00 24.36 C ATOM 1438 CG ASN A 512 −4.980 −2.240 22.1081.00 34.57 C ATOM 1439 OD1 ASN A 512 −3.903 −2.442 22.653 1.00 38.07 OATOM 1440 ND2 ASN A 512 −5.447 =1.024 21.872 1.00 38.61 N ATOM 1441 CASN A 512 −5.973 −5.747 20.953 1.00 30.41 C ATOM 1442 O ASN A 512 −6.100−6.530 21.893 1.00 30.25 D ATOM 1443 N PHE A 513 −6.622 −5.898 19.8041.00 23.64 N ATOM 1444 CA PHE A 513 −7.529 −7.031 19.648 1.00 23.12 CATOM 1445 CB PHE A 513 −8.965 −6.544 19.642 1.00 24.06 C ATOM 1446 CGPHE A 513 −9.365 −5.836 20.901 1.00 33.74 C ATOM 1447 CD1 PHE A 513−9.502 −4.456 20.925 1.00 33.94 C ATOM 1448 CD2 PHE A 513 −9.566 −6.55822.081 1.00 33.20 C ATOM 1449 CE1 PHE A 513 −9.829 −3.790 22.119 1.0040.69 C ATOM 1450 CE2 PHE A 513 −9.894 −5.901 23.267 1.00 39.14 C ATOM1451 CZ PHE A 513 −10.021 −4.517 23.282 1.00 38.17 C ATOM 1452 C PHE A513 −7.299 −7.940 18.447 1.00 26.12 C ATOM 1453 O PHE A 513 −8.122−8.815 18.183 1.00 25.90 O ATOM 1454 N ARG A 514 −6.200 −7.719 17.7151.00 20.92 N ATOM 1455 CA ARG A 514 −5.855 −8.511 16.548 1.00 18.78 CATOM 1456 CB ARG A 514 −5.504 −9.966 16.974 1.00 22.53 C ATOM 1457 CGARG A 514 −4.403 −9.980 18.017 1.00 24.16 C ATOM 1458 CD ARG A 514−3.883 −11.364 18.353 1.00 26.16 C ATOM 1459 NE ARG A 514 −2.727 −11.22919.247 1.00 25.10 N ATOM 1460 CZ ARG A 514 −1.983 −12.248 19.657 1.0027.44 C ATOM 1461 NH1 ARG A 514 −2.269 −13.477 19.264 1.00 27.42 N ATOM1462 NH2 ARG A 514 −0.928 −12.027 20.443 1.00 29.69 N ATOM 1463 C ARG A514 −7.008 −8.520 15.532 1.00 19.73 C ATOM 1464 O ARG A 514 −7.173−9.487 14.790 1.00 21.31 O ATOM 1465 N LYS A 515 −7.733 −7.404 15.4801.00 22.26 N ATOM 1466 CA LYS A 515 −8.891 −7.277 14.597 1.00 19.38 CATOM 1467 CB LYS A 515 −9.995 −6.589 15.385 1.00 23.23 C ATOM 1468 CGLYS A 515 −11.303 −6.407 14.627 1.00 24.88 C ATOM 1469 CD LYS A 515−12.277 −5.554 15.432 1.00 21.97 C ATOM 1470 CE LYS A 515 −13.434 −5.09914.557 1.00 37.46 C ATOM 1471 NZ LYS A 515 −14.341 −4.148 15.261 1.0042.53 N ATOM 1472 C LYS A 515 −8.547 −6.460 13.322 1.00 21.36 C ATOM1473 O LYS A 515 −8.165 −5.303 13.436 1.00 20.92 O ATOM 1474 N PHE A 516−8.740 −7.059 12.143 1.00 21.89 N ATOM 1475 CA PHE A 516 −8.421 −6.38710.870 1.00 21.28 C ATOM 1476 CB PHE A 516 −7.346 −7.180 10.127 1.0020.51 C ATOM 1477 CG PHE A 516 −6.025 −7.215 10.878 1.00 21.58 C ATOM1478 CD1 PHE A 516 −5.857 −8.098 11.954 1.00 23.48 C ATOM 1479 CD2 PHE A516 −4.998 −6.338 10.555 1.00 23.31 C ATOM 1480 CE1 PHE A 516 −4.672−8.099 12.698 1.00 25.88 C ATOM 1481 CE2 PHE A 516 −3.814 −6.334 11.2961.00 24.06 C ATOM 1482 CZ PHE A 516 −3.654 −7.220 12.370 1.00 29.09 CATOM 1483 C PHE A 516 −9.659 −6.196 10.014 1.00 24.42 C ATOM 1484 O PHEA 516 −10.584 −7.031 10.045 1.00 21.09 O ATOM 1485 N SER A 517 −9.648−5.111 9.241 1.00 20.69 N ATOM 1486 CA SER A 517 −10.818 −4.718 8.4341.00 26.64 C ATOM 1487 CB SER A 517 −11.826 −4.042 9.379 1.00 21.54 CATOM 1488 OG SER A 517 −11.213 −2.897 10.008 1.00 22.44 O ATOM 1489 CSER A 517 −10.377 −3.679 7.393 1.00 21.26 C ATOM 1490 O SER A 517 −9.236−3.288 7.397 1.00 19.96 O ATOM 1491 N SER A 518 −11.287 −3.223 6.5291.00 19.99 N ATOM 1492 CA SER A 518 −10.873 −2.180 5.589 1.00 20.05 CATOM 1493 CB SER A 518 −12.002 −1.884 4.584 1.00 27.16 C ATOM 1494 OGSER A 518 −12.033 −2.959 3.646 1.00 30.81 O ATOM 1495 C SER A 518−10.473 −0.946 6.366 1.00 19.52 C ATOM 1496 O SER A 518 −9.591 −0.1965.937 1.00 26.21 O ATOM 1497 N ARG A 519 −11.119 −0.725 7.500 1.00 22.21N ATOM 1498 CA ARG A 519 −10.780 0.414 8.311 1.00 18.10 C ATOM 1499 CBARG A 519 −11.842 0.646 9.371 1.00 22.77 C ATOM 1500 CG ARG A 519−13.023 1.415 8.764 1.00 25.96 C ATOM 1501 CD ARG A 519 −14.180 1.4259.709 1.00 34.85 C ATOM 1502 NE ARG A 519 −15.279 2.180 9.131 1.00 42.62N ATOM 1503 CZ ARG A 519 −16.510 2.180 9.633 1.00 49.29 C ATOM 1504 NH1ARG A 519 −16.798 1.484 10.727 1.00 43.62 N ATOM 1505 NH2 ARG A 519−17.458 2.899 9.031 1.00 50.64 N ATOM 1506 C ARG A 519 −9.393 0.3438.939 1.00 20.79 C ATOM 1507 O ARG A 519 −8.808 1.403 9.221 1.00 20.53 OATOM 1508 N SER A 520 −8.877 −0.867 9.182 1.00 18.48 N ATOM 1509 CA SERA 520 −7.508 −0.904 9.705 1.00 19.17 C ATOM 1510 CB SER A 520 −7.177−2.264 10.410 1.00 17.39 C ATOM 1511 OG SER A 520 −7.348 −3.401 9.6031.00 22.96 O ATOM 1512 C SER A 520 −6.586 −0.607 8.484 1.00 18.94 C ATOM1513 O SER A 520 −5.506 −0.023 8.631 1.00 21.65 O ATOM 1514 N ASP A 521−7.032 −0.960 7.272 1.00 19.22 N ATOM 1515 CA ASP A 521 −6.261 −0.6576.038 1.00 23.13 C ATOM 1516 CB ASP A 521 −6.902 −1.257 4.770 1.00 27.96C ATOM 1517 CG ASP A 521 −6.488 −2.716 4.501 1.00 23.02 C ATOM 1518 OD1ASP A 521 −5.536 −3.223 5.145 1.00 22.00 O ATOM 1519 OD2 ASP A 521−7.113 −3.347 3.598 1.00 23.07 O ATOM 1520 C ASP A 521 −6.253 0.8775.874 1.00 18.27 C ATOM 1521 O ASP A 521 −5.238 1.473 5.445 1.00 20.55 OATOM 1522 N VAL A 522 −7.366 1.525 6.246 1.00 16.95 N ATOM 1523 CA VAL A522 −7.421 3.004 6.168 1.00 16.30 C ATOM 1524 CB VAL A 522 −8.833 3.5346.537 1.00 18.70 C ATOM 1525 CG1 VAL A 522 −8.820 5.066 6.757 1.00 19.08C ATOM 1526 CG2 VAL A 522 −9.801 3.174 5.395 1.00 15.77 C ATOM 1527 CVAL A 522 −6.361 3.620 7.093 1.00 20.10 C ATOM 1528 O VAL A 522 −5.6704.569 6.711 1.00 19.37 O ATOM 1529 N TRP A 523 −6.210 3.069 8.294 1.0019.01 N ATOM 1530 CA TRP A 523 −5.186 3.593 9.216 1.00 17.00 C ATOM 1531CB TRP A 523 −5.240 2.819 10.551 1.00 16.75 C ATOM 1532 CG TRP A 523−4.247 3.339 11.594 1.00 17.47 C ATOM 1533 CD2 TRP A 523 −4.561 4.07812.781 1.00 18.40 C ATOM 1534 CE2 TRP A 523 −3.336 4.384 13.411 1.0019.18 C ATOM 1535 CE3 TRP A 523 −5.763 4.514 13.379 1.00 16.68 C ATOM1536 CD1 TRP A 523 −2.889 3.226 11.559 1.00 22.45 C ATOM 1537 NE1 TRP A523 −2.327 3.856 12.650 1.00 17.34 N ATOM 1538 CZ2 TRP A 523 −3.2675.112 14.607 1.00 20.28 C ATOM 1539 CZ3 TRP A 523 −5.692 5.252 14.5701.00 18.90 C ATOM 1540 CH2 TRP A 523 −4.457 5.536 15.170 1.00 20.73 CATOM 1541 C TRP A 523 −3.799 3.464 8.573 1.00 16.27 C ATOM 1542 O TRP A523 −2.988 4.402 8.628 1.00 19.33 O ATOM 1543 N SER A 524 −3.528 2.3157.952 1.00 17.09 N ATOM 1544 CA SER A 524 −2.231 2.082 7.277 1.00 22.19C ATOM 1545 CB SER A 524 −2.178 0.658 6.722 1.00 21.77 C ATOM 1546 OGSER A 524 −2.247 −0.299 7.751 1.00 31.82 O ATOM 1547 C SER A 524 −2.0083.039 6.114 1.00 23.32 C ATOM 1548 O SER A 524 −0.888 3.499 5.878 1.0017.77 O ATOM 1549 N TYR A 525 −3.076 3.334 5.381 1.00 22.60 N ATOM 1550CA TYR A 525 −3.042 4.279 4.274 1.00 22.61 C ATOM 1551 CB TYR A 525−4.457 4.413 3.642 1.00 20.36 C ATOM 1552 CG TYR A 525 −4.463 5.4022.506 1.00 18.97 C ATOM 1553 CD1 TYR A 525 −3.886 5.077 1.285 1.00 21.53C ATOM 1554 CE1 TYR A 525 −3.835 6.020 0.230 1.00 20.51 C ATOM 1555 CD2TYR A 525 −5.005 6.685 2.673 1.00 20.00 C ATOM 1556 CE2 TYR A 525 −4.9617.620 1.642 1.00 21.87 C ATOM 1557 CZ TYR A 525 −4.376 7.284 0.428 1.0024.64 C ATOM 1558 OH TYR A 525 −4.358 8.214 −0.589 1.00 24.81 O ATOM1559 C TYR A 525 −2.590 5.634 4.815 1.00 18.79 C ATOM 1560 O TYR A 525−1.760 6.319 4.208 1.00 22.11 O ATOM 1561 N GLY A 526 −3.133 6.036 5.9631.00 16.47 N ATOM 1562 CA GLY A 526 −2.737 7.291 6.582 1.00 17.93 C ATOM1563 C GLY A 526 −1.233 7.343 6.852 1.00 20.82 C ATOM 1564 O GLY A 526−0.571 8.366 6.583 1.00 20.21 O ATOM 1565 N VAL A 527 −0.691 6.262 7.4091.00 18.53 N ATOM 1566 CA VAL A 527 0.755 6.202 7.680 1.00 15.75 C ATOM1567 CB VAL A 527 1.109 4.902 8.477 1.00 20.06 C ATOM 1568 CG VAL A 5272.624 4.842 8.768 1.00 18.66 C ATOM 1569 CG1 VAL A 527 0.292 4.842 8.7681.00 18.66 C ATOM 1570 C VAL A 527 1.490 6.249 6.326 1.00 16.40 C ATOM1571 O VAL A 527 2.527 6.888 6.205 1.00 21.73 O ATOM 1572 N THR A 5280.941 5.594 5.307 1.00 19.11 N ATOM 1573 CA THR A 528 1.562 5.595 3.9751.00 18.53 C ATOM 1574 CB THR A 528 0.794 4.663 3.020 1.00 21.20 C ATOM1575 OG1 THR A 528 0.891 3.318 3.519 1.00 21.69 O ATOM 1576 CG2 THR A528 1.392 4.705 1.618 1.00 22.45 C ATOM 1577 C THR A 528 1.587 7.0323.416 1.00 24.70 C ATOM 1578 O THR A 528 2.599 7.456 2.850 1.00 19.73 OATOM 1579 N MET A 529 0.479 7.764 3.587 1.00 19.61 N ATOM 1580 CA MET A529 0.425 9.179 3.143 1.00 19.25 C ATOM 1581 CB MET A 529 −0.902 9.8483.576 1.00 20.84 C ATOM 1582 CG MET A 529 −2.135 9.296 2.846 1.00 22.24C ATOM 1583 SD MET A 529 −3.608 10.284 3.352 1.00 24.00 S ATOM 1584 CEMET A 529 −3.207 11.921 2.622 1.00 23.54 C ATOM 1585 C MET A 529 1.5609.943 3.821 1.00 19.48 C ATOM 1586 O MET A 529 2.276 10.736 3.182 1.0020.92 O ATOM 1587 N TRP A 530 1.724 9.726 5.124 1.00 19.75 N ATOM 1588CA TRP A 530 2.777 10.434 5.882 1.00 18.54 C ATOM 1589 CB TRP A 5302.731 10.069 7.376 1.00 20.48 C ATOM 1590 CG TRP A 530 3.582 10.9448.225 1.00 18.20 C ATOM 1591 CD2 TRP A 530 4.969 10.745 8.527 1.00 18.21C ATOM 1592 CE2 TRP A 530 5.389 11.838 9.336 1.00 19.74 C ATOM 1593 CE3TRP A 530 5.899 9.752 8.197 1.00 20.68 C ATOM 1594 CD1 TRP A 530 3.21412.116 8.842 1.00 18.28 C ATOM 1595 NE1 TRP A 530 4.305 12.661 9.5201.00 22.22 N ATOM 1596 CZ2 TRP A 530 6.712 11.961 9.819 1.00 25.36 CATOM 1597 CZ3 TRP A 530 7.212 9.872 8.681 1.00 22.68 C ATOM 1598 CH2 TRPA 530 7.598 10.969 9.479 1.00 26.97 C ATOM 1599 C TRP A 530 4.171 10.1525.349 1.00 21.37 C ATOM 1600 0 TRP A 530 4.972 11.093 5.118 1.00 22.21 OATOM 1601 N GLU A 531 4.475 8.870 5.161 1.00 22.41 N ATOM 1602 CA GLU A531 5.773 8.443 4.634 1.00 23.01 C ATOM 1603 CB GLU A 531 5.800 6.9384.345 1.00 22.19 C ATOM 1604 CG GLU A 531 5.636 5.990 5.540 1.00 26.83 CATOM 1605 CD GLU A 531 5.699 4.530 5.079 1.00 29.43 C ATOM 1606 OE1 GLUA 531 4.621 3.926 4.848 1.00 23.48 O ATOM 1607 OE2 GLU A 531 6.836 3.9994.621 1.00 26.99 O ATOM 1608 C GLU A 531 6.035 9.114 3.304 1.00 22.15 CATOM 1609 O GLU A 531 7.149 9.587 3.030 1.00 22.47 O ATOM 1610 N ALA A532 5.017 9.120 2.445 1.00 20.60 N ATOM 1611 CA ALA A 532 5.170 9.7101.121 1.00 20.49 C ATOM 1612 CB ALA A 532 3.951 9.366 0.222 1.00 21.29 CATOM 1613 C ALA A 532 5.376 11.209 1.143 1.00 22.68 C ATOM 1614 O ALA A532 6.294 11.721 0.487 1.00 21.66 O ATOM 1615 N LEU A 533 4.523 11.9181.881 1.00 24.52 N ATOM 1616 CA LEU A 533 4.601 13.377 1.597 1.00 27.55C ATOM 1617 CB LEU A 533 3.301 13.951 2.553 1.00 23.33 C ATOM 1618 CGLEU A 533 2.113 13.809 1.586 1.00 24.16 C ATOM 1619 CD1 LEU A 533 0.78414.069 2.314 1.00 30.47 C ATOM 1620 CD2 LEU A 533 2.289 14.808 0.4081.00 26.48 C ATOM 1621 C LEU A 533 5.832 13.849 2.737 1.00 28.49 C ATOM1622 O LEU A 533 6.213 15.021 2.661 1.00 23.09 O ATOM 1623 N SER A 5346.458 12.921 3.462 1.00 23.64 N ATOM 1624 CA SER A 534 7.686 13.2164.218 1.00 24.10 C ATOM 1625 CB SER A 534 7.717 12.409 5.509 1.00 24.84C ATOM 1626 OG SER A 534 6.724 12.875 6.402 1.00 32.38 O ATOM 1627 C SERA 534 8.867 12.778 3.370 1.00 23.66 C ATOM 1628 O SER A 534 10.00412.749 3.839 1.00 26.17 O ATOM 1629 N TYR A 535 8.581 12.408 2.130 1.0023.34 N ATOM 1630 CA TYR A 535 9.593 11.943 1.196 1.00 28.19 C ATOM 1631CB TYR A 535 10.485 13.112 0.733 1.00 28.89 C ATOM 1632 CG TYR A 5359.724 14.020 −0.219 1.00 29.59 C ATOM 1633 CD1 TYR A 535 8.811 14.9390.274 1.00 28.98 C ATOM 1634 CE1 TYR A 535 8.026 15.712 −0.584 1.0030.80 C ATOM 1635 CD2 TYR A 535 9.849 13.887 −1.599 1.00 26.41 C ATOM1636 CE2 TYR A 535 9.063 14.647 −2.472 1.00 29.12 C ATOM 1637 CZ TYR A535 8.155 15.558 −1.948 1.00 23.83 C ATOM 1638 OH TYR A 535 7.383 16.325−2.773 1.00 30.19 O ATOM 1639 C TYR A 535 10.447 10.781 1.709 1.00 32.28C ATOM 1640 O TYR A 535 11.672 10.845 1.691 1.00 27.48 O ATOM 1641 N GLYA 536 9.781 9.722 2.174 1.00 26.27 N ATOM 1642 CA GLY A 536 10.495 8.5302.610 1.00 25.77 C ATOM 1643 C GLY A 536 11.019 8.433 4.022 1.00 30.26 CATOM 1644 O GLY A 536 11.754 7.499 4.353 1.00 37.11 O ATOM 1645 N GLN A537 10.648 9.380 4.876 1.00 30.46 N ATOM 1646 CA GLN A 537 11.080 9.3466.263 1.00 28.02 C ATOM 1647 CB GLN A 537 10.740 10.672 6.935 1.00 34.05C ATOM 1648 CG GLN A 537 11.750 11.776 6.618 1.00 44.08 C ATOM 1649 CDGLN A 537 11.367 13.123 7.203 1.00 46.85 C ATOM 1650 OE1 GLN A 53710.983 13.224 8.371 1.00 55.73 O ATOM 1651 NE2 GLN A 537 11.477 14.1706.394 1.00 50.81 N ATOM 1652 C GLN A 537 10.401 8.188 7.011 1.00 29.96 CATOM 1653 O GLN A 537 9.343 7.715 6.601 1.00 24.20 O ATOM 1654 N LYS A538 11.028 7.722 8.094 1.00 26.82 N ATOM 1655 CA LYS A 538 10.446 6.6388.870 1.00 27.30 C ATOM 1656 CB LYS A 538 11.533 5.871 9.635 1.00 32.27C ATOM 1657 CG LYS A 538 12.495 5.132 8.724 1.00 41.48 C ATOM 1658 CDLYS A 538 13.536 4.359 9.529 1.00 46.01 C ATOM 1659 CE LYS A 538 14.2783.365 8.644 1.00 48.76 C ATOM 1660 NZ LYS A 538 15.278 2.577 9.429 1.0054.95 N ATOM 1661 C LYS A 538 9.431 7.175 9.875 1.00 28.24 C ATOM 1662 OLYS A 538 9.665 8.195 10.529 1.00 28.85 O ATOM 1663 N PRO A 539 8.2836.496 10.008 1.00 24.53 N ATOM 1664 CD PRO A 539 7.742 5.389 9.198 1.0022.29 C ATOM 1665 CA PRO A 539 7.286 6.966 10.972 1.00 24.04 C ATOM 1666CB PRO A 539 6.053 6.118 10.644 1.00 28.10 C ATOM 1667 CG PRO A 5396.644 4.857 10.098 1.00 36.04 C ATOM 1668 C PRO A 539 7.737 6.759 12.4211.00 28.35 C ATOM 1669 O PRO A 539 8.426 5.783 12.734 1.00 25.90 O ATOM1670 N TYR A 540 7.343 7.680 13.292 1.00 23.53 N ATOM 1671 CA TYR A 5407.656 7.645 14.722 1.00 28.38 C ATOM 1672 CB TYR A 540 6.831 6.55515.418 1.00 24.00 C ATOM 1673 CG TYR A 540 5.331 6.586 15.095 1.00 27.38C ATOM 1674 CD1 TYR A 540 4.477 7.452 15.766 1.00 24.16 C ATOM 1675 CE1TYR A 540 3.096 7.476 15.483 1.00 20.41 C ATOM 1676 CD2 TYR A 540 4.8005.746 14.119 1.00 28.23 C ATOM 1677 CE2 TYR A 540 3.417 5.767 13.8001.00 21.95 C ATOM 1678 CZ TYR A 540 2.580 6.632 14.496 1.00 20.01 C ATOM1679 OH TYR A 540 1.244 6.670 14.207 1.00 24.93 O ATOM 1680 C TYR A 5409.136 7.346 14.903 1.00 28.93 C ATOM 1681 O TYR A 540 9.508 6.478 15.6891.00 30.14 O ATOM 1682 N LYS A 541 9.942 8.095 14.152 1.00 27.25 N ATOM1683 CA LYS A 541 11.391 7.985 14.100 1.00 39.82 C ATOM 1684 CB LYS A541 11.939 9.274 13.472 1.00 44.06 C ATOM 1685 CG LYS A 541 13.334 9.16712.893 1.00 54.68 C ATOM 1686 CD LYS A 541 13.699 10.418 12.075 1.0054.79 C ATOM 1687 CE LYS A 541 12.794 10.586 10.848 1.00 59.69 C ATOM1688 NZ LYS A 541 13.234 11.695 9.938 1.00 56.19 N ATOM 1689 C LYS A 54112.074 7.722 15.447 1.00 42.70 C ATOM 1690 O LYS A 541 12.849 6.77715.590 1.00 43.82 O ATOM 1691 N LYS A 542 11.784 8.549 16.433 1.00 44.10N ATOM 1692 CA LYS A 542 12.425 8.378 17.728 1.00 51.46 C ATOM 1693 CBLYS A 542 12.682 9.749 18.350 1.00 51.94 C ATOM 1694 CG LYS A 542 11.42510.565 18.581 1.00 56.75 C ATOM 1695 CD LYS A 542 11.731 11.841 19.3591.00 59.67 C ATOM 1696 CE LYS A 542 10.455 12.559 19.767 1.00 60.04 CATOM 1697 NZ LYS A 542 10.684 13.819 20.538 1.00 63.82 N ATOM 1698 C LYSA 542 11.649 7.512 18.709 1.00 55.84 C ATOM 1699 O LYS A 542 11.7467.724 19.920 1.00 59.11 O ATOM 1700 N MET A 543 10.908 6.523 18.207 1.0041.98 N ATOM 1701 CA MET A 543 10.125 5.658 19.083 1.00 43.90 C ATOM1702 CB MET A 543 8.645 6.029 19.019 1.00 45.70 C ATOM 1703 CG MET A 5438.230 7.209 19.856 1.00 53.80 C ATOM 1704 SD MET A 543 6.477 7.54819.578 1.00 44.32 S ATOM 1705 CE MET A 543 6.609 7.548 19.578 1.00 44.97C ATOM 1706 C MET A 543 10.235 4.185 18.755 1.00 46.16 C ATOM 1707 O META 543 10.497 3.805 17.616 1.00 49.81 O ATOM 1708 N LYS A 544 10.0013.359 19.769 1.00 48.84 N ATOM 1709 CA LYS A 544 10.042 1.909 19.6271.00 54.57 C ATOM 1710 CB LYS A 544 10.872 1.284 20.748 1.00 54.75 CATOM 1711 CG LYS A 544 10.262 1.451 22.134 1.00 63.19 C ATOM 1712 CD LYSA 544 11.076 0.704 23.191 1.00 63.73 C ATOM 1713 CE LYS A 544 10.4000.726 24.560 1.00 65.53 C ATOM 1714 NZ LYS A 544 11.146 −0.103 25.5611.00 62.21 N ATOM 1715 C LYS A 544 8.612 1.374 19.699 1.00 57.82 C ATOM1716 O LYS A 544 7.655 2.112 19.464 1.00 56.73 O ATOM 1717 N GLY A 5458.475 0.096 20.046 1.00 53.41 N ATOM 1718 CA GLY A 545 7.161 −0.51220.128 1.00 51.20 C ATOM 1719 C GLY A 545 6.218 0.124 21.133 1.00 51.82C ATOM 1720 O GLY A 545 5.359 0.915 20.752 1.00 53.88 O ATOM 1721 N PROA 546 6.350 −0.206 22.427 1.00 52.05 N ATOM 1722 CD PRO A 546 7.333−1.165 22.966 1.00 55.28 C ATOM 1723 CA PRO A 546 5.507 0.321 23.5061.00 51.30 C ATOM 1724 CB PRO A 546 6.215 −0.181 24.768 1.00 52.03 CATOM 1725 CG PRO A 546 6.743 −1.503 24.322 1.00 51.79 C ATOM 1726 C PROA 546 5.325 1.835 23.515 1.00 44.10 C ATOM 1727 O PRO A 546 4.296 2.34223.983 1.00 37.86 O ATOM 1728 N GLU A 547 6.329 2.553 23.017 1.00 39.18N ATOM 1729 CA GLU A 547 6.274 4.004 22.973 1.00 45.81 C ATOM 1730 CBGLU A 547 7.607 4.582 22.516 1.00 44.80 C ATOM 1731 CG GLU A 547 8.7604.296 23.450 1.00 60.26 C ATOM 1732 CD GLU A 547 10.033 4.976 23.0011.00 56.95 C ATOM 1733 OE1 GLU A 547 10.093 6.220 23.034 1.00 61.75 OATOM 1734 OE2 GLU A 547 10.970 4.247 22.608 1.00 59.24 O ATOM 1735 C GLUA 547 5.173 4.495 22.030 1.00 31.92 C ATOM 1736 O GLU A 547 4.417 5.38122.384 1.00 33.88 O ATOM 1737 N VAL A 548 5.113 3.922 20.834 1.00 36.76N ATOM 1738 CA VAL A 548 4.097 4.331 19.849 1.00 30.35 C ATOM 1739 CBVAL A 548 4.316 3.610 18.513 1.00 35.20 C ATOM 1740 CG1 VAL A 548 3.2894.083 17.486 1.00 31.70 C ATOM 1741 CG2 VAL A 548 5.723 3.888 18.0161.00 39.20 C ATOM 1742 C VAL A 548 2.678 4.060 20.344 1.00 32.59 C ATOM1743 O VAL A 548 1.801 4.913 20.242 1.00 32.29 O ATOM 1744 N MET A 5492.448 2.874 20.989 1.00 34.32 N ATOM 1745 CA MET A 549 1.131 2.52821.418 1.00 33.89 C ATOM 1746 CB MET A 549 1.171 1.124 22.025 1.00 43.40C ATOM 1747 CG MET A 549 −0.202 0.486 22.120 1.00 54.00 C ATOM 1748 SDMET A 549 −1.061 0.474 20.506 1.00 73.10 S ATOM 1749 CE MET A 549 −2.2391.839 20.656 1.00 53.85 C ATOM 1750 C MET A 549 0.650 3.532 22.476 1.0031.82 C ATOM 1751 O MET A 549 −0.486 4.000 22.436 1.00 30.85 O ATOM 1752N ALA A 550 1.525 3.856 23.420 1.00 30.61 N ATOM 1753 CA ALA A 550 1.1944.791 24.490 1.00 32.54 C ATOM 1754 CB ALA A 550 2.363 4.852 25.488 1.0037.38 C ATOM 1755 C ALA A 550 0.910 6.186 23.911 1.00 27.78 C ATOM 1756O ALA A 550 0.004 6.894 24.362 1.00 28.75 O ATOM 1757 N PHE A 551 1.7116.569 22.920 1.00 26.75 N ATOM 1758 CA PHE A 551 1.595 7.861 22.220 1.0029.08 C ATOM 1759 CB PHE A 551 2.712 7.922 21.157 1.00 21.20 C ATOM 1760CG PHE A 551 2.791 9.219 20.382 1.00 25.99 C ATOM 1761 CD1 PHE A 5513.346 10.358 20.954 1.00 30.16 C ATOM 1762 CD2 PHE A 551 2.370 9.26519.041 1.00 29.19 C ATOM 1763 CE1 PHE A 551 3.497 11.540 20.206 1.0026.26 C ATOM 1764 CE2 PHE A 551 2.521 10.449 18.286 1.00 24.90 C ATOM1765 CZ PHE A 551 3.087 11.577 18.877 1.00 28.07 C ATOM 1766 C PHE A 5510.214 7.955 21.565 1.00 23.03 C ATOM 1767 O PHE A 551 −0.516 8.92221.748 1.00 24.86 O ATOM 1768 N ILE A 552 −0.149 6.931 20.806 1.00 23.91N ATOM 1769 CA ILE A 552 −1.452 6.917 20.145 1.00 23.84 C ATOM 1770 CBILE A 552 −1.559 5.675 19.241 1.00 24.60 C ATOM 1771 CG2 ILE A 552−2.973 5.513 18.716 1.00 26.02 C ATOM 1772 CG1 ILE A 552 −0.476 5.75718.155 1.00 28.63 C ATOM 1773 CD1 ILE A 552 −0.614 6.952 17.164 1.0028.18 C ATOM 1774 C ILE A 552 −2.575 6.921 21.184 1.00 24.71 C ATOM 1775O ILE A 552 −3.565 7.653 21.048 1.00 25.03 O ATOM 1776 N GLU A 553−2.419 6.121 22.238 1.00 26.97 N ATOM 1777 CA GLU A 553 −3.433 6.05523.295 1.00 27.80 C ATOM 1778 CB GLU A 553 −3.040 5.014 24.346 1.0039.68 C ATOM 1779 CG GLU A 553 −3.089 3.573 23.834 1.00 47.86 C ATOM1780 CD GLU A 553 −4.506 3.085 23.586 1.00 47.67 C ATOM 1781 OE1 GLU A553 −4.662 2.019 22.950 1.00 54.95 O ATOM 1782 OE2 GLU A 553 −5.4603.758 24.032 1.00 55.56 O ATOM 1783 C GLU A 553 −3.645 7.424 23.972 1.0027.09 C ATOM 1784 O GLU A 553 −4.757 7.751 24.386 1.00 33.91 O ATOM 1785N GLN A 554 −2.577 8.206 24.088 1.00 30.97 N ATOM 1786 CA GLN A 554−2.639 9.545 24.678 1.00 31.06 C ATOM 1787 CB GLN A 554 −1.232 10.09324.909 1.00 33.93 C ATOM 1788 CG GLN A 554 −0.454 9.441 26.030 1.0047.13 C ATOM 1789 CD GLN A 554 0.949 9.978 26.069 1.00 48.57 C ATOM 1790OE1 GLN A 554 1.159 11.187 25.932 1.00 58.53 O ATOM 1791 NE2 GLN A 5541.921 9.089 26.250 1.00 53.00 N ATOM 1792 C GLN A 554 −3.364 10.53423.767 1.00 34.15 C ATOM 1793 O GLN A 554 −3.599 11.677 24.155 1.0029.68 O ATOM 1794 N GLY A 555 −3.698 10.104 22.552 1.00 28.32 N ATOM1795 CA GLY A 555 −4.389 11.008 21.644 1.00 30.45 C ATOM 1796 C GLY A555 −3.449 11.876 20.805 1.00 27.04 C ATOM 1797 O GLY A 555 −3.85912.914 20.269 1.00 28.32 O ATOM 1798 N LYS A 556 −2.188 11.478 20.6941.00 21.48 N ATOM 1799 CA LYS A 556 −1.240 12.239 19.886 1.00 21.96 CATOM 1800 CB LYS A 556 0.096 12.390 20.618 1.00 22.25 C ATOM 1801 CG LYSA 556 −0.048 13.123 21.964 1.00 24.42 C ATOM 1802 CD LYS A 556 1.31213.380 22.586 1.00 25.86 C ATOM 1803 CE LYS A 556 1.157 14.112 23.9341.00 34.77 C ATOM 1804 NZ LYS A 556 2.485 14.453 24.554 1.00 33.67 NATOM 1805 C LYS A 556 −1.007 11.516 18.567 1.00 23.68 C ATOM 1806 O LYSA 556 −1.140 10.291 18.492 1.00 22.12 O ATOM 1807 N ARG A 557 −0.61012.285 17.548 1.00 19.92 N ATOM 1808 CA ARG A 557 −0.365 11.722 16.2291.00 20.32 C ATOM 1809 CB ARG A 557 −1.575 11.983 15.311 1.00 20.48 CATOM 1810 CG ARG A 557 −2.895 11.354 15.818 1.00 21.21 C ATOM 1811 CDARG A 557 −2.900 9.812 15.730 1.00 19.93 C ATOM 1812 NE ARG A 557 −4.2039.222 16.106 1.00 19.69 N ATOM 1813 CZ ARG A 557 −4.580 8.900 17.3431.00 22.33 C ATOM 1814 NH1 ARG A 557 −3.755 9.098 18.397 1.00 21.75 NATOM 1815 NH2 ARG A 557 −5.771 8.337 17.536 1.00 19.39 N ATOM 1816 C ARGA 557 0.890 12.335 15.616 1.00 20.01 C ATOM 1817 O ARG A 557 1.41913.342 16.131 1.00 21.06 O ATOM 1818 N MET A 558 1.371 11.729 14.5261.00 23.13 N ATOM 1819 CA MET A 558 2.562 12.260 13.862 1.00 24.90 CATOM 1820 CB MET A 558 2.999 11.351 12.710 1.00 20.87 C ATOM 1821 CG META 558 3.673 10.070 13.153 1.00 26.00 C ATOM 1822 SD MET A 558 4.4009.177 11.757 1.00 25.21 S ATOM 1823 CE MET A 558 2.987 8.458 10.949 1.0019.49 C ATOM 1824 C MET A 558 2.287 13.669 13.330 1.00 27.66 C ATOM 1825O MET A 558 1.164 13.992 12.898 1.00 21.51 O ATOM 1826 N GLU A 559 3.32114.503 13.371 1.00 24.36 N ATOM 1827 CA GLU A 559 3.230 15.871 12.9081.00 26.80 C ATOM 1828 CB GLU A 559 4.539 16.613 13.219 1.00 33.66 CATOM 1829 CG GLU A 559 5.822 15.788 12.977 1.00 43.05 C ATOM 1830 CD GLUA 559 6.068 14.712 14.060 1.00 54.97 C ATOM 1831 OE1 GLU A 559 6.46315.072 15.198 1.00 59.07 O ATOM 1832 OE2 GLU A 559 5.867 13.506 13.7441.00 44.76 O ATOM 1833 C GLU A 559 2.939 15.992 11.417 1.00 27.49 C ATOM1834 O GLU A 559 3.209 15.088 10.642 1.00 27.65 O ATOM 1835 N CYS A 5602.387 17.130 11.026 1.00 22.31 N ATOM 1836 CA CYS A 560 2.122 17.3779.616 1.00 23.70 C ATOM 1837 CB CYS A 560 1.293 18.655 9.468 1.00 27.79C ATOM 1838 SG CYS A 560 0.980 19.104 7.751 1.00 30.84 S ATOM 1839 C CYSA 560 3.490 17.535 8.905 1.00 29.44 C ATOM 1840 O CYS A 560 4.350 18.3009.351 1.00 29.36 O ATOM 1841 N PRO A 561 3.733 16.769 7.825 1.00 29.57 NATOM 1842 CD PRO A 561 2.944 15.629 7.312 1.00 26.67 C ATOM 1843 CA PROA 561 5.018 16.890 7.116 1.00 31.79 C ATOM 1844 CB PRO A 561 4.86515.932 5.933 1.00 29.22 C ATOM 1845 CG PRO A 561 3.976 14.837 6.496 1.0025.42 C ATOM 1846 C PRO A 561 5.244 18.319 6.619 1.00 29.76 C ATOM 1847O PRO A 561 4.302 19.055 6.362 1.00 26.53 O ATOM 1848 N PRO A 562 6.50218.728 6.473 1.00 36.98 N ATOM 1849 CD PRO A 562 7.740 18.045 6.884 1.0038.45 C ATOM 1850 CA PRO A 562 6.775 20.085 5.994 1.00 38.46 C ATOM 1851CB PRO A 562 8.302 20.140 5.984 1.00 42.62 C ATOM 1852 CG PRO A 5628.674 19.202 7.102 1.00 47.24 C ATOM 1853 C PRO A 562 6.177 20.293 4.5961.00 36.90 C ATOM 1854 O PRO A 562 6.268 19.415 3.745 1.00 37.38 O ATOM1855 N GLU A 563 5.550 21.445 4.363 1.00 38.19 N ATOM 1856 CA GLU A 5634.968 21.740 3.048 1.00 43.57 C ATOM 1857 CB GLU A 563 6.025 21.5541.944 1.00 50.62 C ATOM 1858 CG GLU A 563 7.282 22.401 2.118 1.00 53.80C ATOM 1859 CD GLU A 563 8.502 21.788 1.429 1.00 62.44 C ATOM 1860 OE1GLU A 563 8.457 21.580 0.193 1.00 63.21 O ATOM 1861 OE2 GLU A 563 9.50421.509 2.131 1.00 64.48 O ATOM 1862 C GLU A 563 3.720 20.924 2.698 1.0044.24 C ATOM 1863 O GLU A 563 3.164 21.068 1.607 1.00 48.48 O ATOM 1864N CYS A 564 3.275 20.048 3.598 1.00 41.39 N ATOM 1865 CA CYS A 564 2.06019.285 3.344 1.00 37.90 C ATOM 1866 CB CYS A 564 1.968 18.064 4.279 1.0037.32 C ATOM 1867 SG CYS A 564 0.438 17.119 4.110 1.00 38.37 S ATOM 1868C CYS A 564 0.884 20.221 3.602 1.00 37.50 C ATOM 1869 O CYS A 564 0.75320.773 4.698 1.00 38.57 O ATOM 1870 N PRO A 565 0.012 20.416 2.597 1.0037.07 N ATOM 1871 CD PRO A 565 0.058 19.780 1.271 1.00 42.57 C ATOM 1872CA PRO A 565 −1.160 21.294 2.716 1.00 33.51 C ATOM 1873 CB PRO A 565−1.791 21.231 1.330 1.00 40.30 C ATOM 1874 CG PRO A 565 −1.369 19.8830.824 1.00 44.48 C ATOM 1875 C PRO A 565 −2.114 20.827 3.792 1.00 35.24C ATOM 1876 O PRO A 565 −2.258 19.622 4.024 1.00 32.71 O ATOM 1877 N PROA 566 −2.800 21.776 4.448 1.00 34.52 N ATOM 1878 CD PRO A 566 −2.69223.231 4.207 1.00 34.66 C ATOM 1879 CA PRO A 566 −3.762 21.487 5.5161.00 30.97 C ATOM 1880 CB PRO A 566 −4.398 22.862 5.795 1.00 34.13 CATOM 1881 CG PRO A 566 −3.308 23.823 5.454 1.00 32.16 C ATOM 1882 C PROA 566 −4.814 20.438 5.135 1.00 34.26 C ATOM 1883 O PRO A 566 −5.14919.585 5.950 1.00 28.40 O ATOM 1884 N GLU A 567 −5.331 20.498 3.902 1.0027.60 N ATOM 1885 CA GLU A 567 −6.367 19.562 3.456 1.00 32.42 C ATOM1886 CB GLU A 567 −6.859 19.918 2.036 1.00 36.27 C ATOM 1887 CG GLU A567 −6.961 21.413 1.739 1.00 49.38 C ATOM 1888 CD GLU A 567 −5.60422.059 1.539 1.00 48.16 C ATOM 1889 OE1 GLU A 567 −4.880 21.658 0.6021.00 63.97 O ATOM 1890 OE2 GLU A 567 −5.259 22.966 2.318 1.00 48.66 OATOM 1891 C GLU A 567 −5.848 18.127 3.440 1.00 27.96 C ATOM 1892 O GLU A567 −6.553 17.189 3.829 1.00 27.68 O ATOM 1893 N LEU A 568 −4.615 17.9682.976 1.00 24.93 N ATOM 1894 CA LEU A 568 −4.002 16.658 2.906 1.00 28.04C ATOM 1895 CB LEU A 568 −2.727 16.761 2.076 1.00 31.66 C ATOM 1896 CGLEU A 568 −2.401 15.622 1.133 1.00 34.34 C ATOM 1897 CD1 LEU A 568−3.680 15.015 0.564 1.00 38.44 C ATOM 1898 CD2 LEU A 568 −1.519 16.1820.013 1.00 25.83 C ATOM 1899 C LEU A 568 −3.700 16.146 4.307 1.00 30.03C ATOM 1900 O LEU A 568 −3.906 14.963 4.591 1.00 26.77 O ATOM 1901 N TYRA 569 −3.199 17.016 5.187 1.00 24.67 N ATOM 1902 CA TYR A 569 −2.94716.354 6.538 1.00 22.81 C ATOM 1903 CB TYR A 569 −2.176 17.572 7.3751.00 21.70 C ATOM 1904 CG TYR A 569 −1.824 17.040 8.753 1.00 21.77 CATOM 1905 CD1 TYR A 569 −0.996 15.920 8.895 1.00 23.70 C ATOM 1906 CE1TYR A 569 −0.720 15.375 10.158 1.00 23.93 C ATOM 1907 CD2 TYR A 569−2.371 17.614 9.912 1.00 26.51 C ATOM 1908 CE2 TYR A 569 −2.107 17.07411.184 1.00 29.40 C ATOM 1909 CZ TYR A 569 −1.288 15.960 11.297 1.0028.24 C ATOM 1910 OH TYR A 569 −1.060 15.430 12.544 1.00 25.64 O ATOM1911 C TYR A 569 −4.270 16.175 7.234 1.00 23.78 C ATOM 1912 O TYR A 569−4.326 15.199 7.999 1.00 22.51 O ATOM 1913 N ALA A 570 −5.339 16.9366.983 1.00 23.61 N ATOM 1914 CA ALA A 570 −6.621 16.634 7.632 1.00 26.10C ATOM 1915 CB ALA A 570 −7.710 17.646 7.202 1.00 26.46 C ATOM 1916 CALA A 570 −7.091 15.225 7.308 1.00 24.49 C ATOM 1917 O ALA A 570 −7.66614.532 8.162 1.00 24.77 O ATOM 1918 N LEU A 571 −6.855 14.806 6.074 1.0023.99 N ATOM 1919 CA LEU A 571 −7.263 13.499 5.589 1.00 21.89 C ATOM1920 CB LEU A 571 −7.092 13.432 4.065 1.00 25.02 C ATOM 1921 CG LEU A571 −7.346 12.049 3.472 1.00 23.70 C ATOM 1922 CD1 LEU A 571 −8.72411.529 3.891 1.00 26.43 C ATOM 1923 CD2 LEU A 571 −7.236 12.135 1.9531.00 26.11 C ATOM 1924 C LEU A 571 −6.406 12.422 6.245 1.00 20.20 C ATOM1925 O LEU A 571 −6.895 11.428 6.757 1.00 21.42 O ATOM 1926 N MET A 572−5.105 12.652 6.205 1.00 21.26 N ATOM 1927 CA MET A 572 −4.141 11.7586.808 1.00 24.72 C ATOM 1928 CB MET A 572 −2.771 12.434 6.700 1.00 30.40C ATOM 1929 CG MET A 572 −1.685 11.742 7.418 1.00 32.31 C ATOM 1930 SDMET A 572 −0.160 12.660 7.265 1.00 26.55 S ATOM 1931 CE MET A 572 −0.16513.232 5.451 1.00 24.24 C ATOM 1932 C MET A 572 −4.531 11.574 8.280 1.0022.05 C ATOM 1933 O MET A 572 −4.607 10.448 8.782 1.00 23.12 O ATOM 1934N SER A 573 −4.796 12.686 8.965 1.00 18.12 N ATOM 1935 CA SER A 573−5.158 12.630 10.390 1.00 21.72 C ATOM 1936 CB SER A 573 −5.155 14.05510.973 1.00 21.94 C ATOM 1937 OG SER A 573 −5.574 14.093 12.330 1.0026.24 O ATOM 1938 C SER A 573 −6.498 11.920 10.625 1.00 26.16 C ATOM1939 O SER A 573 −6.660 11.195 11.599 1.00 21.94 O ATOM 1940 N ASP A 574−7.471 12.122 9.749 1.00 21.50 N ATOM 1941 CA ASP A 574 −8.748 11.4279.902 1.00 22.60 C ATOM 1942 CB ASP A 574 −9.791 11.915 8.883 1.00 20.64C ATOM 1943 CG ASP A 574 −10.331 13.301 9.213 1.00 23.27 C ATOM 1944 OD1ASP A 574 −10.160 13.772 10.360 1.00 22.69 O ATOM 1945 OD2 ASP A 574−10.966 13.888 8.314 1.00 26.93 O ATOM 1946 C ASP A 574 −8.577 9.9029.750 1.00 22.37 C ATOM 1947 O ASP A 574 −9.359 9.141 10.333 1.00 23.59O ATOM 1948 N CYS A 575 −7.583 9.453 8.976 1.00 18.61 N ATOM 1949 CA CYSA 575 −7.339 8.014 8.820 1.00 17.32 C ATOM 1950 CB CYS A 575 −6.2647.728 7.762 1.00 20.93 C ATOM 1951 SG CYS A 575 −6.765 8.124 6.035 1.0023.46 S ATOM 1952 C CYS A 575 −6.855 7.431 10.156 1.00 21.12 C ATOM 1953O CYS A 575 −6.857 6.215 10.343 1.00 19.67 O ATOM 1954 N TRP A 576−6.423 8.322 11.047 1.00 19.87 N ATOM 1955 CA TRP A 576 −5.934 7.93112.370 1.00 21.52 C ATOM 1956 CB TRP A 576 −4.611 8.626 12.709 1.0020.08 C ATOM 1957 CG TRP A 576 −3.521 8.406 11.707 1.00 19.69 C ATOM1958 CD2 TRP A 576 −2.500 9.333 11.360 1.00 16.53 C ATOM 1959 CE2 TRP A576 −1.694 8.716 10.367 1.00 18.10 C ATOM 1960 CE3 TRP A 576 −2.18010.634 11.796 1.00 17.50 C ATOM 1961 CD1 TRP A 576 −3.312 7.284 10.9501.00 20.54 C ATOM 1962 NE1 TRP A 576 −2.207 7.464 10.137 1.00 18.64 NATOM 1963 CZ2 TRP A 576 −0.584 9.357 9.970 1.00 20.52 C ATOM 1964 CZ3TRP A 576 −1.064 11.282 11.231 1.00 19.63 C ATOM 1965 CH2 TRP A 576−0.280 10.638 10.231 1.00 18.57 C ATOM 1966 C TRP A 576 −6.914 8.18513.520 1.00 21.81 C ATOM 1967 O TRP A 576 −6.487 8.424 14.664 1.00 21.51O ATOM 1968 N ILE A 577 −8.211 8.166 13.200 1.00 19.65 N ATOM 1969 CAILE A 577 −9.247 8.325 14.224 1.00 20.80 C ATOM 1970 CB ILE A 577−10.637 8.526 13.566 1.00 22.18 C ATOM 1971 CG2 ILE A 577 −11.783 8.17914.574 1.00 27.26 C ATOM 1972 CG1 ILE A 577 −10.749 9.997 13.091 1.0027.26 C ATOM 1973 CD1 ILE A 577 −11.997 10.298 12.254 1.00 29.41 C ATOM1974 C ILE A 577 −9.194 7.014 15.029 1.00 18.87 C ATOM 1975 O ILE A 577−9.204 5.927 14.455 1.00 21.86 O ATOM 1976 N TYR A 578 −9.099 7.14316.349 1.00 20.88 N ATOM 1977 CA TYR A 578 −8.958 5.973 17.210 1.0025.32 C ATOM 1978 CB TYR A 578 −8.815 6.429 18.672 1.00 23.94 C ATOM1979 CG TYR A 578 −8.350 5.327 19.619 1.00 26.11 C ATOM 1980 CD1 TYR A578 −7.000 5.188 19.946 1.00 31.42 C ATOM 1981 CE1 TYR A 578 −6.5614.141 20.787 1.00 32.15 C ATOM 1982 CD2 TYR A 578 −9.256 4.401 20.1581.00 33.33 C ATOM 1983 CE2 TYR A 578 −8.820 3.354 20.991 1.00 33.06 CATOM 1984 CZ TYR A 578 −7.468 3.232 21.295 1.00 31.77 C ATOM 1985 OH TYRA 578 −7.016 2.178 22.088 1.00 33.01 O ATOM 1986 C TYR A 578 −10.0804.947 17.108 1.00 27.02 C ATOM 1987 O TYR A 578 −9.819 3.750 16.903 1.0022.11 O ATOM 1988 N LYS A 579 −11.313 5.418 17.310 1.00 24.58 N ATOM1989 CA LYS A 579 −12.500 4.583 17.290 1.00 27.83 C ATOM 1990 CB LYS A579 −13.727 5.372 17.776 1.00 29.76 C ATOM 1991 CG LYS A 579 −13.6395.869 19.229 1.00 39.10 C ATOM 1992 CD LYS A 579 −14.979 6.478 19.7091.00 42.19 C ATOM 1993 CE LYS A 579 −14.918 6.879 21.192 1.00 50.93 CATOM 1994 NZ LYS A 579 −16.124 7.694 21.593 1.00 50.31 N ATOM 1995 C LYSA 579 −12.774 4.050 15.904 1.00 29.39 C ATOM 1996 O LYS A 579 −12.9984.803 14.976 1.00 27.65 O ATOM 1997 N TRP A 580 −12.772 2.729 15.8021.00 26.39 N ATOM 1998 CA TRP A 580 −13.012 2.038 14.544 1.00 31.72 CATOM 1999 CB TRP A 580 −13.087 0.542 14.847 1.00 33.80 C ATOM 2000 CGTRP A 580 −13.287 −0.297 13.670 1.00 36.87 C ATOM 2001 CD2 TRP A 580−14.500 −0.948 13.670 1.00 37.12 C ATOM 2002 CE2 TRP A 580 −14.230−0.166 12.097 1.00 42.38 C ATOM 2003 CE3 TRP A 580 −15.792 −0.998 13.8351.00 43.97 C ATOM 2004 CD1 TRP A 580 −12.355 −0.624 12.728 1.00 41.08 CATOM 2005 NE1 TRP A 580 −12.915 −1.452 11.777 1.00 37.64 N ATOM 2006 CZ2TRP A 580 −15.205 −2.428 11.440 1.00 40.07 C ATOM 2007 CZ3 TRP A 580−16.766 −1.757 13.182 1.00 45.16 C ATOM 2008 CH2 TRP A 580 −16.464−2.462 11.996 1.00 48.53 C ATOM 2009 C TRP A 580 −14.297 2.492 13.8471.00 32.01 C ATOM 2010 O TRP A 580 −14.300 2.806 12.651 1.00 29.01 OATOM 2011 N GLU A 581 −15.395 2.528 14.590 1.00 26.90 N ATOM 2012 CA GLUA 581 −16.673 2.930 14.006 1.00 31.38 C ATOM 2013 CB GLU A 581 −17.7852.761 15.043 1.00 42.49 C ATOM 2014 CG GLU A 581 −17.518 1.642 16.0431.00 44.23 C ATOM 2015 CD GLU A 581 −16.725 2.134 17.243 1.00 54.00 CATOM 2016 OE1 GLU A 581 −17.263 2.985 17.997 1.00 62.87 O ATOM 2017 OE2GLU A 581 −15.576 1.686 17.440 1.00 44.35 O ATOM 2018 C GLU A 581−16.703 4.365 13.461 1.00 31.42 C ATOM 2019 O GLU A 581 −17.501 4.67112.585 1.00 32.84 O ATOM 2020 N ASP A 582 −15.824 5.232 13.963 1.0029.31 N ATOM 2021 CA ASP A 582 −15.779 6.631 13.543 1.00 26.27 C ATOM2022 CB ASP A 582 −15.502 7.525 14.759 1.00 30.65 C ATOM 2023 CG ASP A582 −16.611 7.449 15.799 1.00 38.03 C ATOM 2024 OD1 ASP A 582 −17.7417.089 15.416 1.00 34.32 O ATOM 2025 OD2 ASP A 582 −16.357 7.744 16.9891.00 35.77 O ATOM 2026 C ASP A 582 −14.741 6.955 12.458 1.00 28.97 CATOM 2027 O ASP A 582 −14.682 8.086 11.957 1.00 25.58 O ATOM 2028 N ARGA 583 −13.926 5.970 12.107 1.00 26.36 N ATOM 2029 CA ARG A 583 −12.8836.195 11.108 1.00 26.57 C ATOM 2030 CB ARG A 583 −11.756 5.153 11.3131.00 24.45 C ATOM 2031 CG ARG A 583 −10.396 5.437 10.597 1.00 21.69 CATOM 2032 CD ARG A 583 −9.414 4.259 10.869 1.00 18.39 C ATOM 2033 NE ARGA 583 −9.289 4.015 12.315 1.00 17.34 N ATOM 2034 CZ ARG A 583 −9.0812.825 12.866 1.00 21.68 C ATOM 2035 NH1 ARG A 583 −8.963 1.744 12.1131.00 18.82 N ATOM 2036 NH2 ARG A 583 −9.029 2.717 14.200 1.00 22.38 NATOM 2037 C ARG A 583 −13.525 6.070 9.720 1.00 24.67 C ATOM 2038 O ARG A583 −14.382 5.223 9.485 1.00 25.78 O ATOM 2039 N PRO A 584 −13.109 6.9168.769 1.00 23.39 N ATOM 2040 CD PRO A 584 −12.146 8.027 8.893 1.00 25.28C ATOM 2041 CA PRO A 584 −13.667 6.869 7.407 1.00 25.72 C ATOM 2042 CBPRO A 584 −13.073 8.097 6.736 1.00 26.27 C ATOM 2043 CG PRO A 584−11.760 8.276 7.437 1.00 22.96 C ATOM 2044 C PRO A 584 −13.318 5.6096.620 1.00 26.41 C ATOM 2045 O PRO A 584 −12.329 4.940 6.930 1.00 23.65O ATOM 2046 N ASP A 585 −14.142 5.313 5.610 1.00 20.71 N ATOM 2047 CAASP A 585 −13.920 4.182 4.714 1.00 20.68 C ATOM 2048 CB ASP A 585−15.258 3.578 4.236 1.00 31.23 C ATOM 2049 CG ASP A 585 −16.100 3.0425.380 1.00 41.40 C ATOM 2050 OD1 ASP A 585 −15.581 2.249 6.197 1.0048.33 O ATOM 2051 OD2 ASP A 585 −17.295 3.419 5.453 1.00 55.79 O ATOM2052 C ASP A 585 −13.183 4.695 3.471 1.00 19.99 C ATOM 2053 O ASP A 585−13.097 5.907 3.256 1.00 24.11 O ATOM 2054 N PHE A 586 −12.692 3.7772.636 1.00 21.55 N ATOM 2055 CA PHE A 586 −11.960 4.193 1.439 1.00 25.44C ATOM 2056 CB PHE A 586 −11.231 3.013 0.780 1.00 23.78 C ATOM 2057 CGPHE A 586 −9.909 2.689 1.445 1.00 21.80 C ATOM 2058 CD1 PHE A 586 −8.8373.578 1.392 1.00 26.67 C ATOM 2059 CD2 PHE A 586 −9.754 1.480 2.146 1.0026.93 C ATOM 2060 CE1 PHE A 586 −7.606 3.261 2.026 1.00 19.00 C ATOM2061 CE2 PHE A 586 −8.546 1.175 2.767 1.00 22.77 C ATOM 2062 CZ PHE A586 −7.482 2.056 2.701 1.00 20.88 C ATOM 2063 C PHE A 586 −12.863 4.8940.430 1.00 25.78 C ATOM 2064 O PHE A 586 −12.399 5.669 −0.358 1.00 22.13O ATOM 2065 N LEU A 587 −14.168 4.268 0.487 1.00 27.35 N ATOM 2066 CALEU A 587 −15.082 5.342 −0.410 1.00 27.54 C ATOM 2067 CB LEU A 587−16.525 4.916 −0.107 1.00 33.35 C ATOM 2068 CG LEU A 587 −17.649 5.418−1.010 1.00 40.50 C ATOM 2069 CD1 LEU A 587 −17.775 6.902 −0.854 1.0043.82 C ATOM 2070 CD2 LEU A 587 −17.358 5.069 −2.455 1.00 41.16 C ATOM2071 C LEU A 587 −14.879 6.856 −0.178 1.00 21.74 C ATOM 2072 O LEU A 587−14.638 7.596 −1.137 1.00 29.01 O ATOM 2073 N THR A 588 −14.923 7.3221.077 1.00 21.57 N ATOM 2074 CA THR A 588 −14.718 8.743 1.326 1.00 25.49C ATOM 2075 CB THR A 588 −15.271 9.205 2.705 1.00 35.32 C ATOM 2076 OG1THR A 588 −14.462 8.694 3.759 1.00 46.78 O ATOM 2077 CG2 THR A 588−16.687 8.707 2.879 1.00 33.61 C ATOM 2078 C THR A 588 −13.257 9.1531.212 1.00 28.40 C ATOM 2079 O THR A 588 −12.964 10.229 0.705 1.00 26.45O ATOM 2080 N VAL A 589 −12.341 8.293 1.670 1.00 22.28 N ATOM 2081 CAVAL A 589 −10.927 8.646 1.549 1.00 19.94 C ATOM 2082 CB VAL A 589−10.021 7.525 2.161 1.00 27.25 C ATOM 2083 CG1 VAL A 589 −8.539 7.7701.790 1.00 22.69 C ATOM 2084 CG2 VAL A 589 −10.180 7.525 3.673 1.0024.26 C ATOM 2085 C VAL A 589 −10.502 8.911 0.102 1.00 20.96 C ATOM 2086O VAL A 589 −9.788 9.888 −0.178 1.00 21.66 O ATOM 2087 N GLU A 590−10.932 8.047 −0.818 1.00 23.06 N ATOM 2088 CA GLU A 590 −10.583 8.205−2.227 1.00 22.93 C ATOM 2089 CB GLU A 590 −11.130 7.022 −3.049 1.0024.91 C ATOM 2090 CG GLU A 590 −10.775 7.021 −4.559 1.00 27.15 C ATOM2091 CD GLU A 590 −11.603 8.014 −5.414 1.00 31.97 C ATOM 2092 OE1 GLU A590 −12.804 8.214 −5.130 1.00 31.00 O ATOM 2093 OE2 GLU A 590 −11.0568.562 −6.399 1.00 29.57 O ATOM 2094 C GLU A 590 −11.137 9.531 −2.7841.00 25.86 C ATOM 2095 O GLU A 590 −10.466 10.218 −3.552 1.00 21.69 OATOM 2096 N GLN A 591 −12.362 9.875 −2.394 1.00 24.00 N ATOM 2097 CA GLNA 591 −12.972 11.131 −2.856 1.00 27.84 C ATOM 2098 CB GLN A 591 −14.42611.197 −2.398 1.00 29.39 C ATOM 2099 CG GLN A 591 −15.298 10.136 −2.9931.00 32.75 C ATOM 2100 CD GLN A 591 −16.754 10.334 −2.629 1.00 38.78 CATOM 2101 OE1 GLN A 591 −17.078 11.132 −1.745 1.00 43.77 O ATOM 2102 NE2GLN A 591 −17.636 9.614 −3.302 1.00 44.60 N ATOM 2103 C GLN A 591−12.240 12.361 −2.354 1.00 28.08 C ATOM 2104 O GLN A 591 −12.023 13.332−3.097 1.00 27.52 O ATOM 2105 N ARG A 592 −11.851 12.345 −1.084 1.0024.43 N ATOM 2106 CA ARG A 592 −11.138 13.471 −0.520 1.00 25.06 C ATOM2107 CB ARG A 592 −11.060 13.338 1.004 1.00 25.79 C ATOM 2108 CG ARG A592 −12.433 13.494 1.004 1.00 25.79 C ATOM 2109 CD ARG A 592 −12.41813.215 3.127 1.00 31.24 C ATOM 2110 NE ARG A 592 −11.576 14.162 3.8441.00 25.60 N ATOM 2111 CZ ARG A 592 −11.336 14.096 5.146 1.00 25.97 CATOM 2112 NH1 ARG A 592 −11.883 13.123 5.859 1.00 27.29 N ATOM 2113 NH2ARG A 592 −10.551 14.996 5.720 1.00 28.63 N ATOM 2114 C ARG A 592 −9.75013.563 −1.117 1.00 25.17 C ATOM 2115 O ARG A 592 −9.235 14.667 −1.36026.90 1.00 O ATOM 2116 N MET A 593 −9.138 12.409 −1.368 1.00 23.69 NATOM 2117 CA MET A 593 −7.796 12.416 −1.931 1.00 28.31 C ATOM 2118 CBMET A 593 −7.192 11.000 −1.892 1.00 23.46 C ATOM 2119 CG MET A 593−5.743 10.934 −2.292 1.00 23.46 C ATOM 2120 SD MET A 593 −4.646 11.896−1.177 1.00 28.98 S ATOM 2121 CE MET A 593 −3.866 12.944 −2.359 1.0026.58 C ATOM 2122 C MET A 593 −7.862 12.937 −3.372 1.00 26.14 C ATOM2123 O MET A 593 −6.998 13.697 −3.802 1.00 28.83 O ATOM 2124 N ARG A 594−8.877 12.519 −4.117 1.00 23.87 N ATOM 2125 CA ARG A 594 −9.023 12.958−5.498 1.00 24.90 C ATOM 2126 CB ARG A 594 −10.275 12.328 −6.106 1.0021.24 C ATOM 2127 CG ARG A 594 −10.428 12.694 −7.596 1.00 25.80 C ATOM2128 CD ARG A 594 −11.817 12.169 −8.118 1.00 36.37 C ATOM 2129 NE ARG A594 −11.832 10.715 −8.236 1.00 43.01 N ATOM 2130 CZ ARG A 594 −11.35310.041 −9.281 1.00 44.29 C ATOM 2131 NH1 ARG A 594 −10.823 10.690−10.313 1.00 45.97 N ATOM 2132 NH2 ARG A 594 −11.387 8.716 −9.289 1.0038.74 N ATOM 2133 C ARG A 594 −9.116 14.494 −5.542 1.00 28.27 C ATOM2134 O ARG A 594 −8.465 15.150 −6.362 1.00 30.97 O ATOM 2135 N ALA A 595−9.911 15.050 −4.637 1.00 30.31 N ATOM 2136 CA ALA A 595 −10.118 16.495−4.530 1.00 34.21 C ATOM 2137 CB ALA A 595 −11.224 16.787 −3.496 1.0032.96 C ATOM 2138 C ALA A 595 −8.834 17.234 −4.161 1.00 36.64 C ATOM2139 O ALA A 595 −8.550 18.300 −4.705 1.00 34.21 O ATOM 2140 N CYS A 596−8.057 16.664 −3.237 1.00 31.92 N ATOM 2141 CA CYS A 596 −6.803 17.277−2.826 1.00 33.56 C ATOM 2142 CB CYS A 596 −6.169 16.505 −1.655 1.0031.86 C ATOM 2143 SG CYS A 596 −7.012 16.710 −0.074 1.00 40.76 S ATOM2144 C CYS A 596 −5.830 17.280 −3.990 1.00 32.72 C ATOM 2145 O CYS A 596−5.155 18.279 −4.245 1.00 31.91 O ATOM 2146 N TYR A 597 −5.747 16.150−4.686 1.00 28.25 N ATOM 2147 CA TYR A 597 −4.832 16.036 −5.814 1.0030.48 C ATOM 2148 CB TYR A 597 −4.881 14.615 −6.389 1.00 31.14 C ATOM2149 CG TYR A 597 −4.225 14.464 −7.742 1.00 31.11 C ATOM 2150 CD1 TYR A597 −2.963 15.000 −7.993 1.00 32.87 C ATOM 2151 CE1 TYR A 597 −2.37014.894 −9.259 1.00 37.85 C ATOM 2152 CD2 TYR A 597 −4.877 13.806 −8.7801.00 34.93 C ATOM 2153 CE2 TYR A 597 −4.298 13.687 −10.047 1.00 41.03 CATOM 2154 CZ TYR A 597 −3.048 12.420 −10.281 1.00 39.13 C ATOM 2155 OHTYR A 597 −2.505 14.165 −11.543 1.00 39.42 O ATOM 2156 C TYR A 597−5.168 17.049 −6.907 1.00 34.57 C ATOM 2157 O TYR A 597 −4.275 17.751−7.421 1.00 33.33 O ATOM 2158 N TYR A 598 −6.446 17.106 −7.261 1.0030.49 N ATOM 2159 CA TYR A 598 −6.921 18.019 −8.298 1.00 40.96 C ATOM2160 CB TYR A 598 −8.427 17.833 −8.532 1.00 38.84 C ATOM 2161 CG TYR A598 −8.800 16.590 −9.316 1.00 41.02 C ATOM 2162 CD1 TYR A 598 −10.13016.335 −9.659 1.00 49.62 C ATOM 2163 CE1 TYR A 598 −10.490 15.170−10.353 1.00 46.11 C ATOM 2164 CD2 TYR A 598 −7.838 15.651 −9.691 1.0046.14 C ATOM 2165 CE2 TYR A 598 −8.182 14.489 −10.399 1.00 45.32 C ATOM2166 CZ TYR A 598 −9.511 14.252 −10.703 1.00 50.82 C ATOM 2167 OH TYR A598 −9.857 13.082 −11.342 1.00 48.64 O ATOM 2168 C TYR A 598 −6.63019.453 −7.903 1.00 44.26 C ATOM 2169 O TYR A 598 −6.255 20.275 −8.7441.00 50.25 O ATOM 2170 N SER A 599 −6.790 19.759 −6.623 1.00 36.48 NATOM 2171 CA SER A 599 −6.525 21.095 −6.1332 1.00 42.68 C ATOM 2172 CBSER A 599 −6.935 21.185 −4.670 1.00 43.70 C ATOM 2173 OG SER A 599−6.732 22.487 −4.171 1.00 57.23 O ATOM 2174 C SER A 599 −5.035 21.427−6.295 1.00 46.61 C ATOM 2175 O SER A 599 −4.663 22.541 −6.686 1.0038.28 O ATOM 2176 N LEU A 600 −4.176 20.459 −6.006 1.00 35.37 N ATOM2177 CA LEU A 600 −2.740 20.681 −6.137 1.00 43.98 C ATOM 2178 CB LEU A600 −1.955 19.613 −5.372 1.00 36.49 C ATOM 2179 CG LEU A 600 −2.11919.658 −3.850 1.00 42.50 C ATOM 2180 CD1 LEU A 600 −1.522 18.409 −3.2291.00 35.50 C ATOM 2181 CD2 LEU A 600 −1.449 20.896 −3.293 1.00 45.68 CATOM 2182 C LEU A 600 −2.301 20.674 −7.587 1.00 41.54 C ATOM 2183 O LEUA 600 −1.381 21.406 −7.965 1.00 46.25 O ATOM 2184 N ALA A 601 −2.96319.850 −8.393 1.00 38.74 N ATOM 2185 CA ALA A 601 −2.648 19.698 −9.8111.00 47.05 C ATOM 2186 CB ALA A 601 −3.470 18.564 −10.404 1.00 45.68 CATOM 2187 C ALA A 601 −2.912 20.997 −10.596 1.00 52.87 C ATOM 2188 O ALAA 601 −2.239 21.306 −11.556 1.00 53.37 O ATOM 2189 N SER A 602 −3.89921.748 −10.094 1.00 51.50 N ATOM 2190 CA SER A 602 −4.266 23.024 −10.6911.00 57.64 C ATOM 2191 CB SER A 602 −5.750 23.293 −10.458 1.00 57.42 CATOM 2192 OG SER A 602 −6.542 22.301 −11.091 1.00 55.95 O ATOM 2193 CSER A 602 −3.428 24.130 −10.054 1.00 59.56 C ATOM 2194 O SER A 602−3.790 25.302 −10.103 1.00 64.84 O ATOM 2195 N LYS A 603 −2.307 23.730−9.459 1.00 63.84 N ATOM 2196 CA LYS A 603 −1.378 24.639 −8.792 1.0065.05 C ATOM 2197 CB LYS A 603 −0.968 25.767 −9.747 1.00 65.01 C ATOM2198 CG LYS A 603 0.509 26.120 −9.697 1.00 65.21 C ATOM 2199 CD LYS A603 0.835 27.209 −10.706 1.00 65.84 C ATOM 2200 CE LYS A 603 2.33427.480 −10.766 1.00 67.72 C ATOM 2201 NZ LYS A 603 2.656 28.634 −11.6591.00 67.84 N ATOM 2202 C LYS A 603 −2.011 25.214 −7.519 1.00 65.66 CATOM 2203 O LYS A 603 −1.435 25.016 −6.424 1.00 67.21 O ATOM 2204 OXTLYS A 603 −3.085 25.847 −7.626 1.00 69.14 O TER 1 LYS A 603 ATOM 2205 CBPHE B 331 23.385 4.944 44.783 1.00 47.38 C ATOM 2206 CG PHE B 331 26.3864.527 43.338 1.00 47.76 C ATOM 2207 CD1 PHE B 331 27.574 4.465 42.6211.00 52.74 C ATOM 2208 CD2 PHE B 331 25.201 4.218 42.689 1.00 47.87 CATOM 2209 CE1 PHE B 331 27.582 4.104 41.283 1.00 48.41 C ATOM 2210 CE2PHE B 331 25.196 3.855 41.347 1.00 52.09 C ATOM 2211 CZ PHE B 331 26.3873.797 41.347 1.00 50.05 C ATOM 2212 C PHE B 331 23.230 6.878 46.363 1.0045.38 C ATOM 2213 O PHE B 331 27.005 6.988 47.313 1.00 49.66 O ATOM 2214N PHE B 331 28.209 6.632 44.860 1.00 48.36 N ATOM 2215 CA PHE B 33126.733 6.417 44.999 1.00 44.38 C ATOM 2216 N LEU B 332 24.933 7.15646.441 1.00 39.16 N ATOM 2217 CA LEU B 332 24.306 7.623 47.678 1.0040.71 C ATOM 2218 CB LEU B 332 23.601 8.967 47.426 1.00 40.95 C ATOM2219 CG LEU B 332 24.412 10.129 46.828 1.00 42.67 C ATOM 2220 CD1 LEU B332 23.451 11.230 46.342 1.00 38.80 C ATOM 2221 CD2 LEU B 332 25.39410.684 47.864 1.00 39.78 C ATOM 2222 C LEU B 332 23.276 6.592 48.1381.00 42.07 C ATOM 2223 O LEU B 332 22.808 5.781 47.347 1.00 39.83 O ATOM2224 N LYS B 333 22.929 6.621 49.423 1.00 42.54 N ATOM 2225 CA LYS B 33321.927 5.699 49.947 1.00 44.61 C ATOM 2226 CB LYS B 333 22.050 5.57151.467 1.00 46.09 C ATOM 2227 CG LYS B 333 23.341 4.930 51.902 1.0050.67 C ATOM 2228 CD LYS B 333 23.230 4.443 53.337 1.00 58.35 C ATOM2229 CE LYS B 333 24.498 3.707 53.764 1.00 59.84 C ATOM 2230 NZ LYS B333 24.351 3.125 55.132 1.00 62.41 N ATOM 2231 C LYS B 333 20.542 6.20649.605 1.00 41.31 C ATOM 2232 O LYS B 333 20.214 7.357 49.888 1.00 39.53O ATOM 2233 N ARG B 334 19.729 5.332 49.021 1.00 36.95 N ATOM 2234 CAARG B 334 18.375 5.682 48.628 1.00 43.46 C ATOM 2235 CB ARG B 334 17.7074.487 47.944 1.00 44.85 C ATOM 2236 CG ARG B 334 16.275 4.735 47.4851.00 43.32 C ATOM 2237 CD ARG B 334 16.238 5.676 46.299 1.00 38.79 CATOM 2238 NE ARG B 334 14.873 5.974 45.879 1.00 37.97 N ATOM 2239 CZ ARGB 334 14.074 6.819 46.509 1.00 38.57 C ATOM 2240 NH1 ARG B 334 14.5057.457 47.595 1.00 36.94 N ATOM 2241 NH2 ARG B 334 12.846 7.038 46.0541.00 42.39 N ATOM 2242 C ARG B 334 17.547 6.103 49.839 1.00 45.57 C ATOM2243 O ARG B 334 16.571 6.845 49.712 1.00 41.28 O ATOM 2244 N ASP B 33517.960 5.619 51.010 1.00 46.31 N ATOM 2245 CA ASP B 335 17.274 5.89852.272 1.00 45.57 C ATOM 2246 CB ASP B 335 17.823 4.969 53.354 1.0051.22 C ATOM 2247 CG ASP B 335 17.911 3.533 52.887 1.00 54.98 C ATOM2248 OD1 ASP B 335 16.856 2.869 52.816 1.00 60.53 O ATOM 2249 OD2 ASP B335 19.032 3.074 52.567 1.00 62.94 O ATOM 2250 C ASP B 335 17.439 7.33852.719 1.00 42.46 C ATOM 2251 O ASP B 335 16.647 7.840 53.525 1.00 36.68O ATOM 2252 N ASN B 336 18.471 8.010 52.219 1.00 29.28 N ATOM 2253 CAASN B 336 18.713 9.383 52.603 1.00 31.89 C ATOM 2254 CB ASN B 336 20.2119.667 52.652 1.00 33.88 C ATOM 2255 CG ASN B 336 20.904 8.875 53.7341.00 49.73 C ATOM 2256 OD1 ASN B 336 20.356 8.676 54.822 1.00 46.67 OATOM 2257 ND2 ASN B 336 22.124 8.437 53.457 1.00 47.83 N ATOM 2258 C ASNB 336 18.054 10.366 51.655 1.00 27.35 C ATOM 2259 O ASN B 336 18.18811.571 51.819 1.00 28.55 O ATOM 2260 N LEU B 337 17.341 9.834 50.6791.00 31.14 N ATOM 2261 CA LEU B 337 16.687 10.667 49.677 1.00 34.02 CATOM 2262 CB LEU B 337 17.174 10.263 48.277 1.00 30.37 C ATOM 2263 CGLEU B 337 16.623 11.013 47.049 1.00 29.39 C ATOM 2264 CD1 LEU B 33717.255 12.379 46.971 1.00 29.26 C ATOM 2265 CD2 LEU B 337 16.949 10.24645.775 1.00 25.80 C ATOM 2266 C LEU B 337 15.163 10.583 49.728 1.0029.91 C ATOM 2267 O LEU B 337 14.581 9.510 49.799 1.00 30.87 O ATOM 2268N LEU B 338 14.516 11.733 49.674 1.00 26.54 N ATOM 2269 CA LEU B 33813.060 11.780 49.667 1.00 26.34 C ATOM 2270 CB LEU B 338 12.534 12.52450.910 1.00 27.85 C ATOM 2271 CG LEU B 338 10.999 12.521 51.023 1.0029.64 C ATOM 2272 CD1 LEU B 338 10.508 11.097 51.215 1.00 34.52 C ATOM2273 CD2 LEU B 338 10.550 13.388 52.184 1.00 27.72 C ATOM 2274 C LEU B338 12.693 12.562 48.397 1.00 29.11 C ATOM 2275 O LEU B 338 12.94113.762 48.321 1.00 29.08 O ATOM 2276 N ILE B 339 12.145 11.868 47.4021.00 29.57 N ATOM 2277 CA ILE B 339 11.785 12.534 46.150 1.00 28.48 CATOM 2278 CB ILE B 339 11.902 11.564 44.950 1.00 32.66 C ATOM 2279 CG2ILE B 339 11.633 12.331 43.627 1.00 32.51 C ATOM 2280 CG1 ILE B 33913.286 10.909 44.961 1.00 32.18 C ATOM 2281 CD1 ILE B 339 13.495 9.84943.902 1.00 41.01 C ATOM 2282 C ILE B 339 10.366 13.062 46.208 1.0031.19 C ATOM 2283 O ILE B 339 9.431 12.309 46.466 1.00 33.54 O ATOM 2284N ALA B 340 10.208 14.358 45.965 1.00 28.66 N ATOM 2285 CA ALA B 3408.880 14.966 45.989 1.00 34.20 C ATOM 2286 CB ALA B 340 8.990 16.46246.265 1.00 32.40 C ATOM 2287 C ALA B 340 8.152 14.717 44.667 1.00 36.35C ATOM 2288 O ALA B 340 8.775 14.336 43.663 1.00 35.42 O ATOM 2289 N ASPB 341 6.836 14.907 44.674 1.00 33.98 N ATOM 2290 CA ASP B 341 6.04114.711 43.469 1.00 39.65 C ATOM 2291 CB ASP B 341 4.631 14.226 43.8401.00 45.61 C ATOM 2292 CG ASP B 341 3.912 13.554 42.670 1.00 57.27 CATOM 2293 OD1 ASP B 341 4.096 14.002 41.519 1.00 59.44 O ATOM 2294 OD2ASP B 341 3.149 12.582 42.901 1.00 63.51 O ATOM 2295 C ASP B 341 5.95916.070 42.779 1.00 44.29 C ATOM 2296 O ASP B 341 4.868 16.568 42.5021.00 45.33 O ATOM 2297 N ILE B 342 7.119 16.671 42.514 1.00 36.54 N ATOM2298 CA ILE B 342 7.202 17.981 41.879 1.00 36.97 C ATOM 2299 CB ILE B342 7.661 19.043 42.896 1.00 38.63 C ATOM 2300 CG2 ILE B 342 7.85220.397 42.215 1.00 42.84 C ATOM 2301 CG1 ILE B 342 6.645 19.131 44.0331.00 39.67 C ATOM 2302 CD1 ILE B 342 7.093 20.032 45.166 1.00 46.12 CATOM 2303 C ILE B 342 8.225 17.899 40.753 1.00 37.86 C ATOM 2304 O ILE B342 9.336 17.438 40.961 1.00 33.45 O ATOM 2305 N GLU B 343 7.840 18.33539.561 1.00 31.27 N ATOM 2306 CA GLU B 343 8.736 18.281 38.415 1.0035.65 C ATOM 2307 CB GLU B 343 7.994 17.733 37.194 1.00 35.13 C ATOM2308 CG GLU B 343 8.842 17.680 35.940 1.00 40.36 C ATOM 2309 CD GLU B343 8.204 16.874 34.824 1.00 49.77 C ATOM 2310 OE1 GLU B 343 8.17315.627 34.926 1.00 48.98 O ATOM 2311 OE2 GLU B 343 7.734 17.488 33.8451.00 50.13 O ATOM 2312 C GLU B 343 9.287 19.661 38.122 1.00 35.92 C ATOM2313 O GLU B 343 8.522 20.568 37.825 1.00 33.14 O ATOM 2314 N LEU B 34410.612 19.811 38.179 1.00 26.19 N ATOM 2315 CA LEU B 344 11.245 21.10037.907 1.00 26.71 C ATOM 2316 CB LEU B 344 12.646 21.179 38.577 1.0025.66 C ATOM 2317 CG LEU B 344 12.593 21.025 40.097 1.00 30.64 C ATOM2318 CD1 LEU B 344 14.017 20.874 40.644 1.00 27.22 C ATOM 2319 CD2 LEU B344 11.877 22.223 40.737 1.00 33.34 C ATOM 2320 C LEU B 344 11.37321.299 36.404 1.00 25.27 C ATOM 2321 O LEU B 344 11.313 22.428 35.9121.00 30.00 O ATOM 2322 N GLY B 345 11.576 20.206 35.672 1.00 24.88 NATOM 2323 CA GLY B 345 11.683 20.297 34.228 1.00 29.60 C ATOM 2324 C GLYB 345 11.779 18.915 33.635 1.00 29.46 C ATOM 2325 O GLY B 345 11.72017.929 34.336 1.00 32.49 O ATOM 2326 N CYS B 346 11.915 18.818 32.3151.00 27.20 N ATOM 2327 CA CYS B 346 12.057 17.510 31.688 1.00 32.81 CATOM 2328 CB CYS B 346 10.690 16.909 31.391 1.00 41.74 C ATOM 2329 SGCYS B 346 9.815 17.890 30.185 1.00 44.47 S ATOM 2330 C CYS B 346 12.84317.626 30.391 1.00 38.59 C ATOM 2331 O CYS B 346 13.184 18.728 29.9631.00 36.63 O ATOM 2332 N GLY B 347 13.120 16.478 29.785 1.00 36.78 NATOM 2333 CA GLY B 347 13.846 16.426 28.528 1.00 36.32 C ATOM 2334 C GLYB 347 13.362 15.050 27.936 1.00 37.34 C ATOM 2335 O GLY B 347 12.88814.252 28.505 1.00 35.37 O ATOM 2336 N ASN B 348 14.274 14.760 26.8121.00 38.30 N ATOM 2337 CA ASN B 348 14.143 13.451 26.180 1.00 41.78 CATOM 2338 CB ASN B 348 14.905 13.414 24.850 1.00 50.03 C ATOM 2339 CGASN B 348 14.269 14.284 23.799 1.00 55.15 C ATOM 2340 OD1 ASN B 34813.105 14.090 23.440 1.00 59.57 O ATOM 2341 ND2 ASN B 348 15.028 15.25623.289 1.00 59.33 N ATOM 2342 C ASN B 348 14.670 12.334 27.077 1.0039.62 C ATOM 2343 O ASN B 348 14.281 11.183 26.930 1.00 38.79 O ATOM2344 N PHE B 349 15.565 12.683 28.002 1.00 34.25 N ATOM 2345 CA PHE B349 16.144 11.700 28.915 1.00 36.33 C ATOM 2346 CB PHE B 349 17.40812.277 29.580 1.00 38.59 C ATOM 2347 CG PHE B 349 17.140 13.471 30.4591.00 35.63 C ATOM 2348 CD1 PHE B 349 16.529 13.315 31.702 1.00 37.36 CATOM 2349 CD2 PHE B 349 17.441 14.759 30.022 1.00 35.00 C ATOM 2350 CE1PHE B 349 16.216 14.431 32.496 1.00 36.08 C ATOM 2351 CE2 PHE B 34917.135 15.872 30.805 1.00 39.51 C ATOM 2352 CZ PHE B 349 16.518 15.70732.047 1.00 34.21 C ATOM 2353 C PHE B 349 15.156 11.303 30.014 1.0034.30 C ATOM 2354 O PHE B 349 15.219 10.212 30.562 1.00 37.30 O ATOM2355 N GLY B 350 14.263 12.220 30.358 1.00 34.85 N ATOM 2356 CA GLY B350 13.316 11.949 31.422 1.00 32.42 C ATOM 2357 C GLY B 350 12.91913.235 32.096 1.00 33.80 C ATOM 2358 O GLY B 350 12.575 14.204 31.4331.00 38.01 O ATOM 2359 N SER B 351 12.954 13.274 33.421 1.00 34.81 NATOM 2360 CA SER B 351 12.560 14.497 34.079 1.00 31.64 C ATOM 2361 CBSER B 351 11.114 14.395 34.536 1.00 42.24 C ATOM 2362 OG SER B 35110.994 13.473 35.583 1.00 38.56 O ATOM 2363 C SER B 351 13.461 14.85935.246 1.00 24.48 C ATOM 2364 O SER B 351 14.303 14.076 35.670 1.0031.02 O ATOM 2365 N VAL B 352 13.276 16.064 34.751 1.00 23.21 N ATOM2366 CA VAL B 352 14.069 16.551 36.869 1.00 25.51 C ATOM 2367 CB VAL B352 14.776 17.865 36.521 1.00 23.36 C ATOM 2368 CG1 VAL B 352 15.57018.356 37.728 1.00 28.15 C ATOM 2369 CG2 VAL B 352 15.710 17.645 35.3161.00 25.42 C ATOM 2370 C VAL B 352 13.051 16.809 37.964 1.00 25.74 CATOM 2371 O VAL B 352 12.153 17.661 37.818 1.00 26.16 O ATOM 2372 N ARGB 353 13.208 16.078 39.059 1.00 22.97 N ATOM 2373 CA ARG B 353 12.29916.161 40.194 1.00 23.75 C ATOM 2374 CB ARG B 353 11.909 14.745 40.6521.00 25.68 C ATOM 2375 CG ARG B 353 11.121 13.891 39.655 1.00 41.51 CATOM 2376 CD ARG B 353 9.703 14.400 39.449 1.00 48.70 C ATOM 2377 NE ARGB 353 8.746 13.308 39.273 1.00 58.71 N ATOM 2378 CZ ARG B 353 8.25812.560 40.623 1.00 59.20 C ATOM 2379 NH1 ARG B 353 8.627 12.776 41.5191.00 53.03 N ATOM 2380 NH2 ARG B 353 7.404 11.579 39.992 1.00 59.16 NATOM 2381 C ARG B 353 12.924 16.882 41.366 1.00 29.40 C ATOM 2382 O ARGB 353 14.147 16.866 41.554 1.00 30.85 O ATOM 2383 N GLN B 354 12.08617.506 42.178 1.00 26.67 N ATOM 2384 CA GLN B 354 12.580 18.193 43.3611.00 23.26 C ATOM 2385 CB GLN B 354 11.648 19.339 43.751 1.00 25.56 CATOM 2386 CG GLN B 354 12.166 20.151 44.923 1.00 30.39 C ATOM 2387 CDGLN B 354 11.363 21.415 45.160 1.00 38.39 C ATOM 2388 OE1 GLN B 35410.625 21.870 44.288 1.00 35.27 O ATOM 2389 NE2 GLN B 354 11.523 22.00446.341 1.00 39.36 N ATOM 2390 C GLN B 354 12.589 17.139 44.470 1.0027.58 C ATOM 2391 O GLN B 354 11.786 16.188 44.441 1.00 27.31 O ATOM2392 N GLY B 355 13.496 17.303 45.431 1.00 24.17 N ATOM 2393 CA GLY B355 13.551 16.367 46.542 1.00 26.73 C ATOM 2394 C GLY B 355 14.38816.954 47.667 1.00 29.41 C ATOM 2395 O GLY B 355 14.773 18.123 47.6261.00 24.83 O ATOM 2396 N VAL B 356 14.6651 16.125 48.684 1.00 29.40 NATOM 2397 CA VAL B 356 15.476 16.534 49.817 1.00 27.26 C ATOM 2398 CBVAL B 356 14.633 16.754 51.105 1.00 32.61 C ATOM 2399 CG1 VAL B 35615.549 17.148 52.284 1.00 32.35 C ATOM 2400 CG2 VAL B 356 13.611 17.82250.855 1.00 32.47 C ATOM 2401 C VAL B 356 16.446 15.389 50.059 1.0021.33 C ATOM 2402 O VAL B 356 16.077 14.233 49.936 1.00 25.09 O ATOM2403 N TYR B 357 17.690 15.724 50.382 1.00 29.52 N ATOM 2404 CA TYR B357 18.705 14.706 50.643 1.00 30.43 C ATOM 2405 CB TYR B 357 19.85214.784 49.631 1.00 35.80 C ATOM 2406 CG TYR B 357 20.948 13.782 49.9181.00 33.13 C ATOM 2407 CD1 TYR B 357 20.784 12.426 49.633 1.00 34.25 CATOM 2408 CE1 TYR B 357 21.789 11.496 49.933 1.00 38.44 C ATOM 2409 CD2TYR B 357 22.135 14.192 50.510 1.00 40.34 C ATOM 2410 CE2 TYR B 35723.143 13.274 50.816 1.00 39.74 C ATOM 2411 CZ TYR B 357 22.964 11.93550.524 1.00 39.72 C ATOM 2412 OH TYR B 357 23.971 11.048 50.819 1.0049.57 O ATOM 2413 C TYR B 357 19.266 14.944 52.034 1.00 33.64 C ATOM2414 O TYR B 357 19.528 16.085 52.420 1.00 32.19 O ATOM 2415 N ARG B 35819.461 13.863 52.777 1.00 39.19 N ATOM 2416 CA ARG B 358 19.975 13.99054.133 1.00 42.57 C ATOM 2417 CB ARG B 358 19.248 13.003 55.061 1.0040.77 C ATOM 2418 CG ARG B 358 19.743 13.027 56.509 1.00 46.82 C ATOM2419 CD ARG B 358 18.942 12.054 57.364 1.00 45.02 C ATOM 2420 NE ARG B358 18.989 10.695 56.828 1.00 44.71 N ATOM 2421 CZ ARG B 358 18.0759.765 57.089 1.00 45.22 C ATOM 2422 NH1 ARG B 358 17.048 10.048 57.8751.00 46.71 N ATOM 2423 NH2 ARG B 358 18.184 8.548 56.564 1.00 47.43 NATOM 2424 C ARG B 358 21.475 13.760 54.228 1.00 37.12 C ATOM 2425 O ARGB 358 21.957 12.680 53.901 1.00 38.27 O ATOM 2426 N MET B 359 22.19814.798 54.643 1.00 48.39 N ATOM 2427 CA MET B 359 23.641 14.713 54.8541.00 52.85 C ATOM 2428 CB MET B 359 24.368 15.892 54.211 1.00 56.92 CATOM 2429 CG MET B 359 24.070 16.084 52.741 1.00 60.92 C ATOM 2430 SDMET B 359 25.113 17.339 51.987 1.00 69.39 S ATOM 2431 CE MET B 35924.465 18.838 52.768 1.00 66.46 C ATOM 2432 C MET B 359 23.745 14.82056.371 1.00 57.53 C ATOM 2433 O MET B 359 23.423 15.866 59.936 1.0066.72 O ATOM 2434 N ARG B 360 24.163 13.741 57.024 1.00 61.83 N ATOM2435 CA ARG B 360 24.269 13.706 58.488 1.00 63.23 C ATOM 2436 CB ARG B360 25.166 12.537 58.925 1.00 63.83 C ATOM 2437 CG ARG B 360 24.59011.170 58.552 1.00 65.58 C ATOM 2438 CD ARG B 360 23.197 11.000 59.1581.00 65.50 C ATOM 2439 NE ARG B 360 22.294 10.220 58.310 1.00 64.72 NATOM 2440 CZ ARG B 360 22.467 8.936 57.995 1.00 63.90 C ATOM 2441 NH1ARG B 360 23.523 8.261 58.451 1.00 62.73 N ATOM 2442 NH2 ARG B 36021.573 8.317 57.233 1.00 62.15 N ATOM 2443 C ARG B 360 24.765 15.00859.099 1.00 61.92 C ATOM 2444 O ARG B 360 25.971 15.181 59.320 1.0068.74 O ATOM 2445 N LYS B 361 23.811 15.905 59.374 1.00 58.30 N ATOM2446 CA LYS B 361 24.045 17.233 59.984 1.00 55.64 C ATOM 2447 CB LYS B361 25.338 17.844 59.389 1.00 60.30 C ATOM 2448 CG LYS B 361 25.33418.061 57.877 1.00 60.80 C ATOM 2449 CD LYS B 361 26.738 18.379 57.3881.00 63.13 C ATOM 2450 CE LYS B 361 27.334 19.641 57.964 1.00 63.56 CATOM 2451 NZ LYS B 361 28.715 19.918 57.453 1.00 66.04 N ATOM 2452 C LYSB 361 22.857 18.139 59.589 1.00 60.03 C ATOM 2453 O LYS B 361 22.40818.968 60.395 1.00 59.15 O ATOM 2454 N LYS B 362 22.353 17.971 58.3651.00 53.10 N ATOM 2455 CA LYS B 362 21.225 18.756 57.878 1.00 55.57 CATOM 2456 CB LYS B 362 21.661 20.202 57.665 1.00 57.57 C ATOM 2457 CGLYS B 362 22.780 20.355 56.656 1.00 54.04 C ATOM 2458 CD LYS B 36223.226 21.799 56.608 1.00 58.13 C ATOM 2459 CE LYS B 362 24.111 22.04955.408 1.00 60.20 C ATOM 2460 NZ LYS B 362 25.278 21.126 55.386 1.0060.23 N ATOM 2461 C LYS B 362 20.659 18.192 56.571 1.00 48.43 C ATOM2462 O LYS B 362 21.259 17.329 55.945 1.00 47.21 O ATOM 2463 N GLN B 36319.490 18.675 56.168 1.00 51.49 N ATOM 2464 CA GLN B 363 18.877 18.20054.935 1.00 49.86 C ATOM 2465 CB GLN B 363 17.463 17.662 55.190 1.0056.81 C ATOM 2466 CG GLN B 363 17.400 16.534 56.212 1.00 54.91 C ATOM2467 CD GLN B 363 16.007 15.927 56.325 1.00 55.16 C ATOM 2468 OE1 GLN B363 15.000 16.600 56.098 1.00 61.00 O ATOM 2469 NE2 GLN B 363 15.94714.658 56.692 1.00 58.13 N ATOM 2470 C GLN B 363 18.824 19.341 53.9431.00 48.03 C ATOM 2471 O GLN B 363 18.369 20.435 54.261 1.00 50.07 OATOM 2472 N ILE B 364 19.287 19.079 52.727 1.00 39.54 N ATOM 2473 CA ILEB 364 19.294 20.120 51.725 1.00 40.83 C ATOM 2474 CB ILE B 364 20.69920.335 51.165 1.00 45.38 C ATOM 2475 CG2 ILE B 364 21.653 20.714 52.2901.00 41.39 C ATOM 2476 CG1 ILE B 364 21.174 19.071 50.475 1.00 39.09 CATOM 2477 CD1 ILE B 364 22.299 19.333 49.517 1.00 48.16 C ATOM 2478 CILE B 364 18.361 19.817 50.574 1.00 36.23 C ATOM 2479 O ILE B 364 18.08618.656 50.268 1.00 30.72 O ATOM 2480 N ASP B 365 17.875 20.8700 49.9341.00 35.72 N ATOM 2481 CA ASP B 365 16.983 20.700 48.797 1.00 33.63 CATOM 2482 CB ASP B 365 16.300 22.025 48.483 1.00 37.07 C ATOM 2483 CGASP B 365 15.425 22.506 49.621 1.00 43.21 C ATOM 2484 OD1 ASP B 36514.589 21.712 50.105 1.00 44.93 O ATOM 2485 OD2 ASP B 365 15.576 23.67850.026 1.00 47.38 O ATOM 2486 C ASP B 365 17.825 20.269 47.590 1.0029.49 C ATOM 2487 O ASP B 365 18.899 20.819 47.363 1.00 32.88 O ATOM2488 N VAL B 366 17.340 19.303 48.816 1.00 24.92 N ATOM 2489 CA VAL B366 18.080 18.847 45.654 1.00 25.63 C ATOM 2490 CB VAL B 366 18.71817.443 45.885 1.00 22.38 C ATOM 2491 CG1 VAL B 366 19.793 17.506 46.9931.00 22.29 C ATOM 2492 CG2 VAL B 366 17.619 16.405 46.205 1.00 24.67 CATOM 2493 C VAL B 366 17.190 18.731 44.420 1.00 23.28 C ATOM 2494 O VALB 366 15.974 18.745 44.522 1.00 26.31 O ATOM 2495 N ALA B 367 17.81618.653 43.250 1.00 23.51 N ATOM 2496 CA ALA B 367 17.091 18.439 42.0101.00 26.78 C ATOM 2497 CB ALA B 367 19.396 19.567 40.990 1.00 25.36 CATOM 2498 C ALA B 367 17.639 17.074 41.554 1.00 26.08 C ATOM 2499 O ALAB 367 18.843 16.821 41.602 1.00 30.40 O ATOM 2500 N ILE B 368 16.75116.192 41.128 1.00 25.61 N ATOM 2501 CA ILE B 368 17.124 14.839 40.7351.00 25.37 C ATOM 2502 CB ILE B 368 16.365 13.781 41.603 1.00 28.96 CATOM 2503 CG2 ILE B 368 16.853 12.365 41.280 1.00 26.27 C ATOM 2504 CG1ILE B 368 16.580 14.082 43.092 1.00 26.82 C ATOM 2505 CD1 ILE B 36815.300 14.229 43.893 1.00 35.04 C ATOM 2506 C ILE B 368 16.796 14.54839.284 1.00 23.83 C ATOM 2507 O ILE B 368 15.638 14.575 38.895 1.0024.17 O ATOM 2508 N LYS B 369 17.820 14.261 38.491 1.00 25.66 N ATOM2509 CA LYS B 369 17.593 13.923 37.089 1.00 26.48 C ATOM 2510 CB LYS B369 18.853 14.235 36.278 1.00 26.70 C ATOM 2511 CG LYS B 369 18.72713.997 34.804 1.00 32.20 C ATOM 2512 CD LYS B 369 20.014 14.364 34.0941.00 31.43 C ATOM 2513 CE LYS B 369 20.013 13.896 32.654 1.00 37.28 CATOM 2514 NZ LYS B 369 21.184 14.385 31.848 1.00 31.40 N ATOM 2515 C LYSB 369 17.250 12.429 37.070 1.00 30.56 C ATOM 2516 O LYS B 369 18.07911.572 37.414 1.00 29.63 O ATOM 2517 N VAL B 370 16.016 12.112 36.7031.00 28.76 N ATOM 2518 CA VAL B 370 15.553 10.730 36.690 1.00 29.89 CATOM 2519 CB VAL B 370 14.192 10.594 17.410 1.00 32.92 C ATOM 2520 CG1VAL B 370 13.824 9.133 37.553 1.00 38.36 C ATOM 2521 CG2 VAL B 37014.235 11.289 38.775 1.00 31.30 C ATOM 2522 C VAL B 370 15.391 10.22232.265 1.00 33.31 C ATOM 2523 O VAL B 370 14.623 10.779 34.484 1.0033.69 O ATOM 2524 N LEU B 371 16.110 9.166 34.921 1.00 32.83 N ATOM 2525CA LEU B 371 15.992 8.614 33.580 1.00 37.54 C ATOM 2526 CB LEU B 37117.164 7.676 33.288 1.00 39.83 C ATOM 2527 CG LEU B 371 18.543 8.32833.234 1.00 40.84 C ATOM 2528 CD1 LEU B 371 19.589 7.261 32.948 1.0041.39 C ATOM 2529 CD2 LEU B 371 18.555 9.402 32.166 1.00 39.75 C ATOM2530 C LEU B 371 14.675 7.853 33.449 1.00 43.14 C ATOM 2531 O LEU B 37114.307 7.075 34.339 1.00 39.21 O ATOM 2532 N LYS B 372 13.978 8.07532.337 1.00 41.93 N ATOM 2533 CA LYS B 372 12.699 7.420 32.080 1.0047.49 C ATOM 2534 CB LYS B 372 12.114 7.917 30.756 1.00 49.29 C ATOM2535 CG LYS B 372 13.009 7.677 29.541 1.00 52.95 C ATOM 2536 CD LYS B372 12.390 8.257 28.275 1.00 54.13 C ATOM 2537 CE LYS B 372 13.254 7.95727.057 1.00 57.77 C ATOM 2538 NZ LYS B 372 12.655 8.487 25.796 1.0061.32 N ATOM 2539 C LYS B 372 12.851 5.900 32.052 1.00 52.52 C ATOM 2540O LYS B 372 13.951 5.378 31.877 1.00 47.39 O ATOM 2541 N GLN B 37311.740 5.193 32.238 1.00 59.30 N ATOM 2542 CA GLN B 373 11.755 3.73332.231 1.00 57.74 C ATOM 2543 CB GLN B 373 10.418 3.197 32.762 1.0064.02 C ATOM 2544 CG GLN B 373 10.377 1.685 32.981 1.00 66.26 C ATOM2545 CD GLN B 373 11.342 1.215 34.063 1.00 70.74 C ATOM 2546 OE1 GLN B373 12.562 1.337 33.924 1.00 69.05 O ATOM 2547 NE GLN B 373 10.795 0.67235.147 1.00 69.07 N ATOM 2548 C GLN B 373 12.005 3.213 30.811 1.00 61.28C ATOM 2549 O GLN B 373 11.441 3.728 29.840 1.00 59.36 O ATOM 2550 N GLYB 374 12.863 2.203 30.692 1.00 60.31 N ATOM 2551 CA GLY B 374 13.1601.645 29.385 1.00 62.87 C ATOM 2552 C GLY B 374 14.425 2.207 28.763 1.0064.46 C ATOM 2553 O GLY B 374 14.792 1.838 27.643 1.00 64.42 O ATOM 2554N THR B 375 15.091 3.101 29.490 1.00 62.61 N ATOM 2555 CA THR B 37516.326 3.722 29.019 1.00 62.15 C ATOM 2556 CB THR B 375 16.913 4.67830.089 1.00 61.37 C ATOM 2557 OG1 THR B 375 16.039 5.799 30.268 1.0057.85 O ATOM 2558 OG2 THR B 375 18.288 5.175 29.671 1.00 61.31 C ATOM2559 C THR B 375 17.374 2.666 28.673 1.00 60.79 C ATOM 2560 O THR B 37517.728 1.835 29.507 1.00 61.50 O ATOM 2561 N GLU B 376 17.867 2.70827.440 1.00 61.17 N ATOM 2562 CA GLU B 376 18.874 1.753 26.990 1.0063.67 C ATOM 2563 CB GLU B 376 19.139 1.933 25.496 1.00 65.15 C ATOM2564 CG GLU B 376 20.120 0.923 24.917 1.00 71.18 C ATOM 2565 CD GLU B376 20.089 0.883 23.398 1.00 73.78 C ATOM 2566 OE1 GLU B 376 20.3801.923 22.758 1.00 72.53 O ATOM 2567 OE2 GLU B 376 19.769 −0.193 22.8431.00 73.05 O ATOM 2568 C GLU B 376 20.169 1.943 27.771 1.00 65.33 C ATOM2569 O GLU B 376 20.642 3.046 28.237 1.00 61.91 O ATOM 2570 N LYS B 37720.940 0.868 27.910 1.00 59.58 N ATOM 2571 CA LYS B 377 22.196 0.92728.644 1.00 61.29 C ATOM 2572 CB LYS B 377 22.896 −0.432 28.608 1.0065.21 C ATOM 2573 CG LYS B 377 24.222 −0.454 29.356 1.00 65.59 C ATOM2574 CD LYS B 377 24.611 −1.872 29.736 1.00 71.26 C ATOM 2575 CE LYS B377 25.867 −1.896 30.599 1.00 70.47 C ATOM 2576 NZ LYS B 377 26.267−3.292 30.962 1.00 72.53 N ATOM 2577 C LYS B 377 23.131 1.993 28.0951.00 59.78 C ATOM 2578 O LYS B 377 23.999 2.497 28.808 1.00 56.95 O ATOM2579 N ALA B 378 22.952 2.329 26.823 1.00 61.07 N ATOM 2580 CA ALA B 37823.777 3.337 26.168 1.00 59.33 C ATOM 2581 CB ALA B 378 23.399 3.43524.695 1.00 59.59 C ATOM 2582 C ALA B 378 23.624 4.703 26.836 1.00 57.38C ATOM 2583 O ALA B 378 24.612 5.376 27.138 1.00 56.25 O ATOM 2584 N ASPB 379 22.380 5.098 27.075 1.00 57.35 N ATOM 2585 CA ASP B 379 22.0946.388 27.691 1.00 59.15 C ATOM 2586 CB ASP B 379 20.650 6.788 27.4161.00 61.51 C ATOM 2587 CG ASP B 379 20.151 6.255 26.088 1.00 68.59 CATOM 2588 OD1 ASP B 379 20.739 6.601 25.035 1.00 70.20 O ATOM 2589 OD2ASP B 379 19.168 5.479 26.098 1.00 70.89 O ATOM 2590 C ASP B 379 22.3416.358 29.197 1.00 56.77 C ATOM 2591 O ASP B 379 22.596 7.392 29.811 1.0053.33 O ATOM 2592 N THR B 380 22.258 5.170 29.790 1.00 52.16 N ATOM 2593CA THR B 380 22.513 5.019 31.215 1.00 53.38 C ATOM 2594 CB THR B 38022.187 3.590 31.684 1.00 53.55 C ATOM 2595 OG1 THR B 380 20.768 3.39131.641 1.00 54.68 O ATOM 2596 OG2 THR B 380 22.683 3.371 33.096 1.0058.07 C ATOM 2597 C THR B 380 23.998 5.295 31.432 1.00 52.60 C ATOM 2598O THR B 380 24.390 5.980 32.374 1.00 48.13 O ATOM 2599 N GLU B 38124.819 4.752 30.540 1.00 46.95 N ATOM 2600 CA GLU B 381 26.260 4.93730.617 1.00 49.11 C ATOM 2601 CB GLU B 381 26.955 4.060 29.573 1.0054.95 C ATOM 2602 CG GLU B 381 28.020 3.129 30.134 1.00 58.45 C ATOM2603 CD GLU B 381 27.442 1.927 30.862 1.00 65.92 C ATOM 2604 OE1 GLU B381 26.790 2.114 31.913 1.00 66.10 O ATOM 2605 OE2 GLU B 381 27.6440.788 30.377 1.00 67.00 O ATOM 2606 C GLU B 381 26.559 6.412 30.343 1.0045.43 C ATOM 2607 O GLU B 381 27.518 6.974 30.864 1.00 40.91 O ATOM 2608N GLU B 382 25.716 7.029 29.525 1.00 43.34 N ATOM 2609 CA GLU B 38225.871 8.435 29.164 1.00 45.73 C ATOM 2610 CB GLU B 382 24.842 8.79528.099 1.00 50.57 C ATOM 2611 CG GLU B 382 24.988 10.184 27.524 1.0055.43 C ATOM 2612 CD GLU B 382 24.064 10.410 26.336 1.00 60.92 C ATOM2613 OE1 GLU B 382 22.825 10.449 26.528 1.00 67.80 O ATOM 2614 OE2 GLU B382 24.580 10.536 25.203 1.00 65.61 O ATOM 2615 C GLU B 382 25.696 9.33130.394 1.00 42.57 C ATOM 2616 O GLU B 382 26.444 10.294 30.587 1.0036.66 O ATOM 2617 N MET B 383 24.700 9.017 31.217 1.00 36.27 N ATOM 2618CA MET B 383 24.482 9.806 31.417 1.00 36.21 C ATOM 2619 CB MET B 38323.116 9.489 33.051 1.00 37.94 C ATOM 2620 CG MET B 383 22.686 10.58034.040 1.00 45.05 C ATOM 2621 SD MET B 383 21.039 10.380 34.434 1.0049.17 S ATOM 2622 CE MET B 383 21.377 9.057 35.776 1.00 31.72 C ATOM2623 C MET B 383 25.602 9.543 33.420 1.00 32.29 C ATOM 2624 O MET B 38325.912 10.389 34.245 1.00 27.76 O ATOM 2625 N MET B 384 26.212 8.36133.362 1.00 32.45 N ATOM 2626 CA MET B 384 27.310 8.076 34.276 1.0034.42 C ATOM 2627 CB MET B 384 27.664 6.588 34.262 1.00 38.83 C ATOM2628 CG MET B 384 26.634 5.702 39.943 1.00 41.15 C ATOM 2629 SD MET B384 26.295 6.179 36.672 1.00 47.37 S ATOM 2630 CE MET B 384 27.936 6.04137.407 1.00 46.98 C ATOM 2631 C MET B 384 28.529 8.911 33.896 1.00 31.48C ATOM 2632 O MET B 384 29.284 9.352 34.762 1.00 31.65 O ATOM 2633 N ARGB 385 28.727 9.133 32.603 1.00 34.67 N ATOM 2634 CA ARG B 385 29.8489.962 32.172 1.00 36.33 C ATOM 2635 CB ARG B 385 30.011 9.926 30.6521.00 37.82 C ATOM 2636 CG ARG B 385 30.687 8.667 30.129 1.00 45.45 CATOM 2637 CD ARG B 385 31.105 8.837 28.665 1.00 46.60 C ATOM 2638 NE ARGB 385 29.969 8.752 27.756 1.00 45.85 N ATOM 2639 CZ ARG B 385 29.3777.610 27.417 1.00 47.08 C ATOM 2640 NH1 ARG B 385 29.823 6.459 27.9131.00 48.61 N ATOM 2641 NH2 ARG B 385 28.342 7.612 26.592 1.00 46.74 NATOM 2642 C ARG B 385 29.596 11.391 32.636 1.00 29.96 C ATOM 2643 O ARGB 385 30.520 12.098 33.021 1.00 33.63 O ATOM 2644 N GLU B 386 28.33011.799 32.612 1.00 30.00 N ATOM 2645 CA GLU B 386 27.948 13.141 33.0511.00 29.80 C ATOM 2646 CB GLU B 386 26.447 13.368 32.790 1.00 27.12 CATOM 2647 CG GLU B 386 25.882 14.720 33.233 1.00 32.18 C ATOM 2648 CDGLU B 386 24.372 14.825 32.961 1.00 35.05 C ATOM 2649 OE1 GLU B 38623.801 13.830 32.475 1.00 34.50 O ATOM 2650 OE2 GLU B 386 23.756 15.89033.251 1.00 35.81 O ATOM 2651 C GLU B 386 28.259 13.298 34.540 1.0028.79 C ATOM 2652 O GLU B 386 28.752 14.350 34.986 1.00 26.92 O ATOM2653 N ALA B 387 27.967 12.253 35.305 1.00 30.29 N ATOM 2654 CA ALA B387 28.223 12.295 36.736 1.00 33.27 C ATOM 2655 CB ALA B 387 27.64411.044 37.421 1.00 30.95 C ATOM 2656 C ALA B 387 29.744 12.398 36.9621.00 36.41 C ATOM 2657 O ALA B 387 30.191 13.182 37.774 1.00 35.19 OATOM 2658 N GLN B 388 30.518 11.614 36.219 1.00 32.50 N ATOM 2659 CA GLNB 388 31.984 11.654 36.367 1.00 37.92 C ATOM 2660 CB GLN B 388 32.64710.664 35.387 1.00 38.99 C ATOM 2661 CG GLN B 388 32.269 9.211 35.6251.00 47.85 C ATOM 2662 CD GLN B 388 32.810 8.279 34.546 1.00 56.30 CATOM 2663 OE1 GLN B 388 34.016 8.248 34.281 1.00 56.71 O ATOM 2664 NE2GLN B 388 31.914 7.514 33.915 1.00 53.14 N ATOM 2665 C GLN B 388 32.54613.060 36.134 1.00 35.03 C ATOM 2666 O GLN B 388 33.442 13.501 36.8411.00 32.27 O ATOM 2667 N ILE B 389 32.015 13.767 35.135 1.00 30.85 NATOM 2668 CA ILE B 389 32.463 15.130 34.840 1.00 25.41 C ATOM 2669 CBILE B 389 31.853 15.645 33.499 1.00 32.74 C ATOM 2670 CG2 ILE B 38932.051 17.159 33.363 1.00 31.69 C ATOM 2671 CG1 ILE B 389 32.505 14.90632.328 1.00 38.87 C ATOM 2672 CD1 ILE B 389 31.893 15.236 30.982 1.0036.36 C ATOM 2673 C ILE B 389 32.072 16.074 35.949 1.00 26.93 C ATOM2674 O ILE B 389 32.872 16.886 36.411 1.00 30.11 O ATOM 2675 N MET B 39030.832 15.978 36.403 1.00 26.48 N ATOM 2676 CA MET B 390 30.398 16.85737.459 1.00 24.57 C ATOM 2677 CB MET B 390 28.906 16.695 37.735 1.0024.91 C ATOM 2678 CG MET B 390 28.002 17.248 36.638 1.00 26.56 C ATOM2679 SD MET B 390 26.239 17.032 37.117 1.00 30.07 S ATOM 2480 CE MET B390 26.009 18.455 38.144 1.00 31.13 C ATOM 2681 C MET B 390 31.18616.563 38.738 1.00 30.37 C ATOM 2682 O MET B 390 31.506 17.484 39.4871.00 29.10 O ATOM 2683 N HIS B 391 31.497 15.286 38.956 1.00 31.09 NATOM 2684 CA HIS B 391 32.243 14.890 40.160 1.00 37.62 C ATOM 2685 CBHIS B 391 32.285 13.358 40.270 1.00 42.66 C ATOM 2686 CG HIS B 39132.831 12.854 41.573 1.00 50.59 C ATOM 2687 CD2 HIS B 391 32.206 12.39742.686 1.00 51.17 C ATOM 2688 ND1 HIS B 391 34.182 12.815 41.850 1.0056.54 N ATOM 2689 CE1 HIS B 391 34.366 12.356 43.076 1.00 56.46 C ATOM2690 NE2 HIS B 391 33.183 12.094 43.605 1.00 57.11 N ATOM 2692 C HIS B391 33.661 15.454 40.155 1.00 43.32 C ATOM 2692 O HIS B 391 34.33815.452 41.182 1.00 47.18 O ATOM 2693 N GLN B 392 34.111 15.941 38.9991.00 39.89 N ATOM 2694 CA GLN B 392 35.449 16.516 38.886 1.00 40.16 CATOM 2695 CB GLN B 392 36.094 16.110 37.557 1.00 42.86 C ATOM 2696 CGGLN B 392 36.181 14.610 37.364 1.00 47.64 C ATOM 2697 CD GLN B 39236.948 14.219 36.129 1.00 50.73 C ATOM 2698 OE1 GLN B 392 38.161 14.40836.058 1.00 60.38 O ATOM 2699 NE2 GLN B 392 36.250 13.664 35.145 1.0048.83 N ATOM 2700 C GLN B 392 35.415 18.031 38.987 1.00 47.76 C ATOM2701 O GLN B 392 36.444 18.689 38.850 1.00 47.76 O ATOM 2702 N LEU B 39334.233 18.586 39.240 1.00 45.72 N ATOM 2703 CA LEU B 393 34.069 20.03439.342 1.00 45.69 C ATOM 2704 CB LEU B 393 32.909 20.491 38.454 1.0044.69 C ATOM 2705 CG LEU B 393 32.913 20.011 37.000 1.00 46.90 C ATOM2706 CD1 LEU B 393 31.656 20.508 36.312 1.00 44.79 C ATOM 2707 CD2 LEU B393 34.153 20.507 36.281 1.00 37.05 C ATOM 2708 C LEU B 393 33.82620.515 40.770 1.00 45.06 C ATOM 2709 O LEU B 393 33.044 19.928 41.5231.00 49.45 O ATOM 2710 N ASP B 394 34.481 21.603 41.151 1.00 43.03 NATOM 2711 CA ASP B 394 34.315 22.133 42.495 1.00 36.00 C ATOM 2712 CBASP B 394 35.432 21.600 43.403 1.00 47.00 C ATOM 2713 CG ASP B 39435.292 22.063 44.844 1.00 52.54 C ATOM 2714 OD1 ASP B 394 36.167 21.70545.668 1.00 55.59 O ATOM 2715 OD2 ASP B 394 34.315 22.774 45.160 1.0047.08 O ATOM 2716 C ASP B 394 34.381 23.640 42.427 1.00 40.50 C ATOM2717 O ASP B 394 35.434 24.247 42.671 1.00 38.62 O ATOM 2718 N ASN B 39533.251 24.254 42.105 1.00 35.95 N ATOM 2719 CA ASN B 395 33.216 25.66941.987 1.00 31.17 C ATOM 2720 CB ASN B 395 33.463 26.092 40.518 1.0025.15 C ATOM 2721 CG ASN B 395 33.595 27.578 40.328 1.00 36.48 C ATOM2722 OD1 ASN B 395 34.673 28.158 40.523 1.00 37.23 O ATOM 2723 ND2 ASN B395 32.497 28.217 39.950 1.00 25.99 N ATOM 2724 C ASN B 395 31.85126.171 42.458 1.00 30.67 C ATOM 2725 O ASN B 395 30.821 25.528 42.1971.00 28.65 O ATOM 2726 N PRO B 396 31.822 27.315 43.147 1.00 27.83 NATOM 2727 CD PRO B 396 32.966 28.068 43.680 1.00 37.81 C ATOM 2728 CAPRO B 396 30.570 27.867 43.655 1.00 26.99 C ATOM 2729 CB PRO B 39631.036 29.053 44.483 1.00 35.20 C ATOM 2730 CG PRO B 396 32.414 28.62044.946 1.00 41.91 C ATOM 2731 C PRO B 396 29.568 28.291 42.579 1.0029.09 C ATOM 2732 O PRO B 396 28.402 28.428 42.865 1.00 26.93 O ATOM2733 N TYR B 397 30.043 28.485 41.343 1.00 24.67 N ATOM 2734 CA TYR B397 29.145 28.956 40.263 1.00 24.00 C ATOM 2735 CB TYR B 397 29.82730.136 39.545 1.00 23.32 C ATOM 2736 CG TYR B 397 30.228 31.229 40.5241.00 26.27 C ATOM 2737 CD1 TYR B 397 31.568 31.425 40.881 1.00 26.92 CATOM 2738 CE1 TYR B 397 31.929 32.379 41.823 1.00 31.33 C ATOM 2739 CD2TYR B 397 29.266 32.024 41.136 1.00 25.87 C ATOM 2740 CE2 TYR B 39729.620 32.987 42.085 1.00 33.47 C ATOM 2741 CZ TYR B 397 30.950 33.15542.426 1.00 34.44 C ATOM 2742 OH TYR B 397 31.263 34.067 43.411 1.0037.25 O ATOM 2743 C TYR B 397 28.694 27.893 39.294 1.00 23.67 C ATOM2744 O TYR B 397 28.286 28.165 38.135 1.00 24.69 O ATOM 2745 N ILE B 39828.755 26.659 39.752 1.00 21.85 N ATOM 2746 CA ILE B 398 28.336 25.51938.991 1.00 26.71 C ATOM 2747 CB ILE B 398 29.567 24.716 38.567 1.0034.69 C ATOM 2748 CG2 ILE B 398 29.165 23.359 38.073 1.00 36.71 C ATOM2749 CG1 ILE B 398 30.332 25.502 37.498 1.00 28.39 C ATOM 2750 CD1 ILE B398 31.737 25.021 37.232 1.00 39.03 C ATOM 2751 C ILE B 398 27.42124.691 39.906 1.00 34.83 C ATOM 2752 O ILE B 398 27.640 24.636 41.1201.00 31.60 O ATOM 2753 N VAL B 399 26.378 24.103 39.333 1.00 26.19 NATOM 2754 CA VAL B 399 25.548 23.243 40.086 1.00 29.92 C ATOM 2755 CBVAL B 399 24.272 22.781 39.232 1.00 30.42 C ATOM 2756 CG1 VAL B 39923.498 21.627 39.946 1.00 29.50 C ATOM 2757 CG2 VAL B 399 23.360 23.96038.970 1.00 31.26 C ATOM 2758 C VAL B 399 26.265 22.016 40.464 1.0034.54 C ATOM 2759 O VAL B 399 26.697 21.269 39.597 1.00 35.65 O ATOM2760 N ARG B 400 26.430 21.805 41.763 1.00 27.76 N ATOM 2761 CA ARG B400 27.227 20.683 42.244 1.00 32.53 C ATOM 2762 CB ARG B 400 27.74420.994 43.658 1.00 38.09 C ATOM 2763 CG ARG B 400 28.606 22.262 43.7871.00 46.29 C ATOM 2764 CD ARG B 400 28.970 22.541 45.262 1.00 46.35 CATOM 2765 NE ARG B 400 29.833 23.711 45.437 1.00 52.96 N ATOM 2766 CZARG B 400 31.116 23.743 45.092 1.00 55.68 C ATOM 2767 NH1 ARG B 40031.675 22.666 44.557 1.00 51.73 N ATOM 2768 NH2 ARG B 400 31.841 24.84745.278 1.00 52.56 N ATOM 2769 C ARG B 400 26.513 19.345 42.256 1.0027.44 C ATOM 2770 O ARG B 400 25.313 19.254 42.507 1.00 28.50 O ATOM2771 N LEU B 401 27.259 18.280 42.006 1.00 27.68 N ATOM 2772 CA LEU B401 26.695 16.948 42.018 1.00 24.03 C ATOM 2773 CB LEU B 401 27.51416.006 41.156 1.00 32.24 C ATOM 2774 CG LEU B 401 27.086 14.540 41.1841.00 29.66 C ATOM 2775 CD1 LEU B 401 25.713 14.354 40.554 1.00 35.88 CATOM 2776 CD2 LEU B 401 28.132 13.737 40.425 1.00 39.27 C ATOM 2777 CLEU B 401 26.745 16.426 43.456 1.00 35.79 C ATOM 2778 O LEU B 401 27.79616.487 44.103 1.00 29.49 O ATOM 2779 N ILE B 402 25.611 15.945 43.9571.00 27.95 N ATOM 2780 CA ILE B 402 25.581 15.368 45.299 1.00 29.27 CATOM 2781 CB ILE B 402 24.154 15.383 45.922 1.00 31.13 C ATOM 2782 CG2ILE B 402 24.188 14.716 47.305 1.00 33.30 C ATOM 2783 CG1 ILE B 40223.650 16.830 46.065 1.00 26.94 C ATOM 2784 CD1 ILE B 402 24.616 17.76346.743 1.00 31.79 C ATOM 2785 C ILE B 402 26.053 13.921 45.119 1.0032.38 C ATOM 2786 O ILE B 402 26.962 13.448 45.812 1.00 31.53 O ATOM2787 N GLY B 403 25.469 13.226 44.157 1.00 27.83 N ATOM 2788 CA GLY B403 25.870 11.853 43.900 1.00 29.46 C ATOM 2789 C GLY B 403 24.89711.150 42.994 1.00 29.35 C ATOM 2790 O GLY B 403 23.934 11.757 42.5371.00 30.33 O ATOM 2791 N VAL B 404 24.145 9.878 42.717 1.00 26.15 N ATOM2792 CA VAL B 404 24.281 8.084 41.865 1.00 28.12 C ATOM 2793 CB VAL B404 25.106 8.273 40.844 1.00 36.04 C ATOM 2794 CG1 VAL B 404 24.1867.397 39.982 1.00 40.40 C ATOM 2795 CG2 VAL B 404 25.911 9.211 39.9821.00 35.87 C ATOM 2796 C VAL B 404 23.519 9.211 42.755 1.00 32.26 C ATOM2797 O VAL B 404 24.052 7.647 43.744 1.00 31.47 O ATOM 2798 N CYS B 40522.277 7.815 42.392 1.00 30.13 N ATOM 2799 CA CYS B 405 21.471 6.87943.177 1.00 35.84 C ATOM 2800 CB CYS B 405 20.408 7.635 43.976 1.0039.61 C ATOM 2810 SG CYS B 405 19.571 6.617 45.215 1.00 43.65 S ATOM2802 C CYS B 405 20.815 5.849 42.258 1.00 41.06 C ATOM 2803 O CYS B 40520.101 6.200 41.320 1.00 38.70 O ATOM 2804 N GLN B 406 21.086 4.57742.510 1.00 41.04 N ATOM 2805 CA GLN B 406 20.529 3.511 41.687 1.0049.92 C ATOM 2806 CB GLN B 406 21.639 2.549 41.250 1.00 53.55 C ATOM2807 CG GLN B 406 21.165 1.355 40.413 1.00 59.57 C ATOM 2808 CD GLN B406 20.378 1.756 39.169 1.00 56.22 C ATOM 2809 OE1 GLN B 406 19.2052.123 39.246 1.00 59.42 O ATOM 2810 NE2 GLN B 406 21.028 1.687 38.0161.00 59.35 N ATOM 2811 C GLN B 406 19.450 2.750 42.446 1.00 53.55 C ATOM2812 O GLN B 406 19.746 1.894 43.273 1.00 56.70 O ATOM 2813 N ALA B 40718.197 3.080 42.163 1.00 56.23 N ATOM 2814 CA ALA B 407 17.069 2.41842.808 1.00 60.79 C ATOM 2815 CB ALA B 407 16.432 3.359 41.742 1.0058.91 C ATOM 2816 C ALA B 407 16.052 20.12 41.742 1.00 58.91 C ATOM 2817O ALA B 407 16.364 1.212 40.856 1.00 57.00 O ATOM 2818 N GLU B 40814.846 2.568 41.821 1.00 55.11 N ATOM 2819 CA GLU B 408 13.806 2.26040.849 1.00 57.75 C ATOM 2820 CB GLU B 408 12.535 3.065 41.147 1.0061.87 C ATOM 2821 CG GLU B 408 12.759 4.562 41.299 1.00 61.03 C ATOM2822 CD GLU B 408 12.938 4.998 42.748 1.00 61.45 C ATOM 2823 OE1 GLU B408 13.788 4.422 43.464 1.00 62.30 O ATOM 2824 OE2 GLU B 408 12.2285.933 43.169 1.00 57.96 O ATOM 2825 C GLU B 408 14.320 2.590 39.452 1.0058.74 C ATOM 2826 O GLU B 408 13.770 2.139 38.444 1.00 61.01 O ATOM 2827N ALA B 409 15.383 3.387 19.408 1.00 58.64 N ATOM 2828 CA ALA B 40916.017 3.788 38.159 1.00 53.23 C ATOM 2829 CB ALA B 409 15.054 4.62137.327 1.00 57.75 C ATOM 2830 C ALA B 409 17.262 4.595 38.518 1.00 48.64C ATOM 2831 O ALA B 409 17.451 4.957 39.682 1.00 41.77 O ATOM 2832 N LEUB 410 18.113 4.859 37.527 1.00 46.67 N ATOM 2833 CA LEU B 410 19.3485.606 37.757 1.00 41.56 C ATOM 2834 CB LEU B 410 20.326 5.370 36.6071.00 41.30 C ATOM 2835 CG LEU B 410 21.745 5.849 36.893 1.00 39.49 CATOM 2836 CD1 LEU B 410 22.282 5.132 38.127 1.00 40.07 C ATOM 2837 CD2LEU B 410 22.628 5.590 35.680 1.00 44.22 C ATOM 2838 C LEU B 410 19.0247.087 37.877 1.00 36.27 C ATOM 2830 O LEU B 410 18.291 7.631 37.068 1.0032.58 O ATOM 2840 N MET B 411 19.579 7.740 38.888 1.00 31.99 N ATOM 2841CA MET B 411 19.277 9.144 39.105 1.00 28.85 C ATOM 2842 CB MET B 41118.272 9.282 40.261 1.00 27.82 C ATOM 2843 CG MET B 411 16.908 8.46740.120 1.00 38.03 C ATOM 2844 SD MET B 411 15.902 8.655 41.550 1.0039.66 S ATOM 2845 CE MET B 411 16.875 7.893 42.769 1.00 39.08 C ATOM2846 C MET B 411 20.518 9.931 39.454 1.00 34.64 C ATOM 2847 O MET B 41121.415 9.412 40.110 1.00 32.86 O ATOM 2848 N LEU B 412 20.576 11.18239.012 1.00 27.07 N ATOM 2849 CA LEU B 412 21.686 12.070 39.353 1.0024.70 C ATOM 2850 CB LEU B 412 22.213 12.819 38.22 1.00 31.40 C ATOM2851 CG LEU B 412 23.072 12.039 37.146 1.00 42.38 C ATOM 2852 CD1 LEU B412 23.695 13.008 36.127 1.00 40.09 C ATOM 2853 CD2 LEU B 412 24.15611.325 37.940 1.00 44.83 C ATOM 2854 C LEU B 412 21.108 13.086 40.3161.00 32.72 C ATOM 2855 O LEU B 412 20.203 13.829 39.930 1.00 25.93 OATOM 2856 N VAL B 413 21.632 13.118 41.552 1.00 25.13 N ATOM 2857 CA VALB 413 21.179 14.048 42.591 1.00 22.67 C ATOM 2858 CB VAL B 413 21.16913.374 43.997 1.00 27.42 C ATOM 2859 CG1 VAL B 413 20.591 14.333 45.0401.00 22.22 C ATOM 2860 CG2 VAL B 413 20.369 12.079 43.932 1.00 27.93 CATOM 2861 C VAL B 413 22.099 15.245 42.627 1.00 26.70 C ATOM 2862 O VALB 413 23.317 15.115 42.869 1.00 28.13 O ATOM 2863 N MET B 414 21.50316.417 42.414 1.00 23.91 N ATOM 2864 CA MET B 414 22.232 17.672 42.3531.00 23.05 C ATOM 2865 CB MET B 414 22.146 18.241 40.9131 1.00 26.27 CATOM 2866 CG MET B 414 22.782 17.373 39.850 1.00 31.80 C ATOM 2867 SDMET B 414 22.187 17.909 38.179 1.00 31.87 S ATOM 2868 CE MET B 41420.682 16.814 38.038 1.00 34.99 C ATOM 2869 C MET B 414 21.683 18.72943.269 1.00 24.82 C ATOM 2870 O MET B 414 20.536 18.646 43.732 1.0026.89 O ATOM 2871 N GLU B 415 22.475 19.767 43.508 1.00 22.82 N ATOM2872 CA GLU B 415 22.008 20.867 44.330 1.00 25.46 C ATOM 2873 CB GLU B415 23.089 21.939 44.500 1.00 38.09 C ATOM 2874 CG GLU B 415 24.38121.466 45.121 1.00 41.76 C ATOM 2875 CD GLU B 415 25.406 22.600 45.1911.00 56.15 C ATOM 2876 OE1 GLU B 415 25.611 23.293 44.153 1.00 43.26 OATOM 2877 OE2 GLU B 415 26.000 22.796 46.279 1.00 53.48 O ATOM 2878 CGLU B 415 20.848 21.511 43.581 1.00 28.34 C ATOM 2879 O GLU B 415 20.81921.496 42.347 1.00 27.84 O ATOM 2880 N MET B 416 19.903 22.079 44.3271.00 28.24 N ATOM 2881 CA MET B 416 18.776 22.739 43.701 1.00 27.37 CATOM 2882 CB MET B 416 17.482 22.444 44.452 1.00 31.26 C ATOM 2883 CGMET B 416 16.245 22.889 43.658 1.00 33.79 C ATOM 2884 SD MET B 41614.717 22.640 44.566 1.00 40.24 S ATOM 2885 CE MET B 416 13.622 23.86343.732 1.00 41.28 C ATOM 2886 C MET B 416 18.989 24.247 43.709 1.0032.53 C ATOM 2887 O MET B 416 19.462 24.797 44.695 1.00 29.31 O ATOM2888 N ALA B 417 18.639 24.900 42.603 1.00 29.63 N ATOM 2889 CA ALA B417 18.724 26.362 42.497 1.00 32.11 C ATOM 2890 CB ALA B 417 19.67626.775 41.365 1.00 31.26 C ATOM 2891 C ALA B 417 17.282 26.779 42.1861.00 32.20 C ATOM 2892 O ALA B 417 16.903 26.933 41.017 1.00 31.90 OATOM 2893 N GLY B 418 16.500 26.924 43.259 1.00 34.38 N ATOM 2894 CA GLYB 418 15.081 27.243 43.183 1.00 36.34 C ATOM 2895 C GLY B 418 14.63028.461 42.398 1.00 34.85 C ATOM 2896 O GLY B 418 13.447 28.598 42.0821.00 34.44 O ATOM 2897 N GLY B 419 15.563 29.359 42.105 1.00 28.57 NATOM 2898 CA GLY B 419 15.208 30.537 41.339 1.00 30.78 C ATOM 2899 C GLYB 419 14.891 30.180 39.897 1.00 33.81 C ATOM 2900 O GLY B 419 14.24530.944 39.202 1.00 32.35 O ATOM 2901 N GLY B 420 15.370 29.032 39.4271.00 30.29 N ATOM 2902 CA GLY B 420 15.091 28.621 38.065 1.00 27.83 CATOM 2903 C GLY B 420 15.930 29.299 36.980 1.00 24.88 C ATOM 2904 O GLYB 420 16.843 30.054 37.303 1.00 24.54 O ATOM 2905 N PRO B 421 15.61729.068 35.694 1.00 26.97 N ATOM 2906 CD PRO B 421 14.445 28.280 35.2561.00 26.58 C ATOM 2907 CA PRO B 421 16.320 29.631 34.534 1.00 26.79 CATOM 2908 CB PRO B 421 15.508 29.113 33.335 1.00 31.97 C ATOM 2909 CGPRO B 421 14.810 27.921 33.845 1.00 32.59 C ATOM 2910 C PRO B 421 16.40031.148 34.507 1.00 31.93 C ATOM 2911 O PRO B 421 15.430 31.851 34.8011.00 26.82 O ATOM 2912 N LEU B 422 17.570 31.643 34.112 1.00 24.30 NATOM 2913 CA LEU B 422 17.848 33.064 34.025 1.00 25.19 C ATOM 2914 CBLEU B 422 19.316 33.263 33.632 1.00 26.63 C ATOM 2915 CG LEU B 42219.835 34.685 33.470 1.00 27.37 C ATOM 2916 CD1 LEU B 422 19.814 35.39434.801 1.00 28.60 C ATOM 2917 CD2 LEU B 422 21.251 34.623 32.917 1.0025.74 C ATOM 2918 C LEU B 422 16.966 33.799 33.003 1.00 22.35 C ATOM2919 O LEU B 422 16.524 34.916 33.268 1.00 27.34 O ATOM 2920 N HIS B 42316.753 33.207 31.835 1.00 23.59 N ATOM 2921 CA HIS B 423 15.944 33.88430.829 1.00 33.17 C ATOM 2922 CB HIS B 423 15.899 33.099 29.518 1.0033.79 C ATOM 2923 CG HIS B 423 15.322 31.725 29.650 1.00 30.44 C ATOM2924 CD2 HIS B 423 15.309 30.856 30.688 1.00 33.89 C ATOM 2925 ND1 HIS B423 14.631 31.109 28.626 1.00 40.96 N ATOM 2926 CD1 HIS B 423 14.22229.919 29.029 1.00 35.92 C ATOM 2927 NE2 HIS B 423 14.621 29.740 30.2761.00 37.97 N ATOM 2928 C HIS B 423 14.525 34.142 31.341 1.00 37.06 CATOM 2929 O HIS B 423 13.989 35.236 31.153 1.00 39.39 O ATOM 2930 N LYSB 424 13.927 33.149 31.995 1.00 28.98 N ATOM 2931 CA LYS B 424 12.57633.351 32.510 1.00 31.22 C ATOM 2932 CB LYS B 424 11.957 32.006 32.8831.00 28.63 C ATOM 2933 CG LYS B 424 11.695 31.136 31.674 1.00 29.72 CATOM 2934 CD LYS B 424 11.076 29.800 32.117 1.00 42.69 C ATOM 2935 CELYS B 424 10.935 28.829 30.955 1.00 47.20 C ATOM 2936 NZ LYS B 424 9.94927.753 31.294 1.00 54.05 N ATOM 2937 C LYS B 424 12.554 34.296 33.7001.00 33.37 C ATOM 2938 O LYS B 424 11.608 35.064 33.878 1.00 28.31 OATOM 2939 N PHE B 425 13.602 34.269 34.519 1.00 28.20 N ATOM 2940 CA PHEB 425 13.660 35.137 35.681 1.00 26.95 C ATOM 2941 CB PHE B 425 14.89034.802 36.540 1.00 31.21 C ATOM 2942 CG PHE B 425 15.042 35.680 37.7471.00 32.76 C ATOM 2943 CD1 PHE B 425 14.318 35.431 38.904 1.00 41.67 CATOM 2944 CD2 PHE B 425 15.886 36.782 37.710 1.00 35.66 C ATOM 2945 CE1PHE B 425 14.429 36.272 40.011 1.00 40.79 C ATOM 2946 CE2 PHE B 42516.010 37.631 38.805 1.00 43.64 C ATOM 2947 CZ PHE B 425 15.277 37.37739.962 1.00 45.58 C ATOM 2948 C PHE B 425 13.713 36.629 35.310 1.0028.99 C ATOM 2949 O PHE B 425 13.149 37.468 36.010 1.00 28.02 O ATOM2950 N LEU B 426 14.379 36.961 34.212 1.00 27.54 N ATOM 2951 CA LEU B426 14.522 38.373 33.838 1.00 23.94 C ATOM 2952 CB LEU B 426 15.83838.577 33.072 1.00 25.46 C ATOM 2953 CG LEU B 426 17.102 38.323 33.9051.00 23.52 C ATOM 2954 CD1 LEU B 426 18.345 38.424 33.014 1.00 25.22 CATOM 2955 CD2 LEU B 426 17.165 39.329 35.029 1.00 28.05 C ATOM 2956 CLEU B 426 13.368 38.959 33.019 1.00 28.74 C ATOM 2957 O LEU B 426 13.23640.186 32.937 1.00 26.14 O ATOM 2958 N VAL B 427 12.553 38.100 32.4151.00 27.70 N ATOM 2959 CA VAL B 427 11.442 38.584 31.583 1.00 30.96 CATOM 2960 CB VAL B 427 10.577 37.409 31.059 1.00 35.17 C ATOM 2961 CG1VAL B 427 9.323 37.939 30.343 1.00 34.67 C ATOM 2962 CG2 VAL B 42711.391 36.561 30.082 1.00 31.17 C ATOM 2963 C VAL B 427 10.551 39.58132.331 1.00 36.19 C ATOM 2964 O VAL B 427 9.984 39.269 33.386 1.00 37.99O ATOM 2965 N GLY B 428 10.454 40.791 31.788 1.00 44.92 N ATOM 2966 CAGLY B 428 9.637 41.830 32.397 1.00 39.36 C ATOM 2967 C GLY B 428 10.14442.432 33.696 1.00 46.68 C ATOM 2968 A GLY B 428 9.384 43.091 34.4101.00 43.86 O ATOM 2969 N LYS B 429 11.419 42.231 34.019 1.00 36.36 NATOM 2970 CA LYS B 429 11.960 42.772 35.258 1.00 41.33 C ATOM 2971 CBLYS B 429 12.561 41.638 36.068 1.00 45.43 C ATOM 2972 CG LYS B 42911.519 40.599 36.492 1.00 48.96 C ATOM 2973 CD LYS B 429 11.975 39.80437.699 1.00 53.23 C ATOM 2974 CE LYS B 429 11.004 38.680 38.025 1.0052.24 C ATOM 2975 NZ LYS B 429 11.552 37.819 39.108 1.00 60.84 N ATOM2976 C LYS B 429 12.990 43.880 35.028 1.00 42.92 C ATOM 2977 O LYS B 42913.841 44.152 35.883 1.00 41.32 O ATOM 2978 N ARG B 430 12.889 44.53533.878 1.00 38.04 N ATOM 2979 CA ARG B 430 13.824 45.954 33.532 1.0050.47 C ATOM 2980 CB ARG B 430 13.541 46.091 32.116 1.00 52.47 C ATOM2981 CG ARG B 430 14.669 46.918 31.520 1.00 63.31 C ATOM 2982 CD ARG B430 14.548 47.014 29.999 1.00 63.30 C ATOM 2983 NE ARG B 430 15.85746.896 29.351 1.00 63.29 N ATOM 2984 CZ ARG B 430 16.061 46.254 28.2031.00 68.48 C ATOM 2985 NH1 ARG B 430 15.043 45.680 27.573 1.00 63.45 NATOM 2986 NH2 ARG B 430 17.294 46.151 27.698 1.00 66.07 N ATOM 2987 CARG B 430 13.774 46.754 34.518 1.00 53.77 C ATOM 2988 O ARG B 430 14.72747.516 36.643 1.00 53.09 O ATOM 2989 N GLU B 431 12.661 46.879 35.2351.00 54.55 N ATOM 2990 CA GLU B 431 12.518 47.959 36.196 1.00 55.49 CATOM 2991 CB GLU B 431 11.167 48.658 36.020 1.00 57.64 C ATOM 2992 CGGLU B 431 11.104 49.556 34.797 1.00 61.36 C ATOM 2993 CD GLU B 431 9.93250.515 34.839 1.00 66.74 C ATOM 2994 OE1 GLU B 431 9.882 51.356 35.7671.00 71.47 O ATOM 2995 OE2 GLU B 431 9.062 50.433 33.946 1.00 68.60 OATOM 2996 C GLU B 431 12.683 47.510 37.635 1.00 56.39 C ATOM 2997 O GLUB 431 12.608 48.325 38.550 1.00 57.92 O ATOM 2998 N GLU B 432 12.91046.218 37.844 1.00 51.06 N ATOM 2999 CA GLU B 432 13.091 45.720 39.1941.00 50.31 C ATOM 3000 CB GLU B 432 11.992 44.713 39.554 1.00 56.46 CATOM 3001 CG GLU B 432 12.301 43.274 39.217 1.00 60.14 C ATOM 3002 CDGLU B 432 11.319 42.313 39.866 1.00 63.83 C ATOM 3003 OE1 GLU B 43210.118 42.313 39.866 1.00 63.83 O ATOM 3004 OE2 GLU B 432 11.746 41.50140.719 1.00 66.50 O ATOM 3005 C GLU B 432 14.464 45.083 39.364 1.0049.21 C ATOM 3006 O GLU B 432 14.932 44.892 40.483 1.00 47.48 O ATOM3007 N ILE B 433 15.111 44.756 38.246 1.00 43.34 N ATOM 3008 CA ILE B433 16.442 44.156 38.288 1.00 35.43 C ATOM 3009 CB ILE B 433 16.43642.734 37.688 1.00 40.48 C ATOM 3010 CG2 ILE B 433 17.842 42.125 37.7541.00 33.02 C ATOM 3011 CG1 ILE B 433 15.463 41.850 38.460 1.00 39.44 CATOM 3012 CD1 ILE B 433 15.862 41.633 39.896 1.00 42.99 C ATOM 3013 CILE B 433 17.335 45.049 37.446 1.00 37.58 C ATOM 3014 O ILE B 433 17.30944.975 36.217 1.00 33.88 O ATOM 3015 N PRO B 434 18.125 45.919 38.0971.00 33.22 N ATOM 3016 CD PRO B 434 18.093 46.179 39.546 1.00 39.68 CATOM 3017 CA PRO B 434 19.038 46.857 37.435 1.00 37.36 C ATOM 3018 CBPRO B 434 19.661 47.606 38.614 1.00 36.58 C ATOM 3019 CG PRO B 43418.559 47.616 39.604 1.00 47.33 C ATOM 3020 C PRO B 434 20.083 46.16336.578 1.00 35.02 C ATOM 3021 O PRO B 434 20.382 44.986 36.785 1.0029.87 O ATOM 3022 N VAL B 435 20.644 46.904 35.625 1.00 30.90 N ATOM3023 CA VAL B 435 21.699 46.349 34.750 1.00 33.32 C ATOM 3024 CB VAL B435 22.138 47.391 33.699 1.00 32.31 C ATOM 3025 CG1 VAL B 435 23.25546.802 32.839 1.00 32.23 C ATOM 3026 CG2 VAL B 435 20.968 47.792 32.8211.00 38.32 C ATOM 3027 C VAL B 435 22.862 45.875 32.570 1.00 31.88 CATOM 3028 O VAL B 435 23.504 44.873 35.218 1.00 26.54 O ATOM 3029 N SERB 436 23.165 46.593 36.652 1.00 28.96 N ATOM 3030 CA SER B 436 24.27846.225 37.519 1.00 29.85 C ATOM 3031 CB SER B 436 24.437 47.262 38.6461.00 33.71 C ATOM 3032 OG SER B 436 23.246 47.361 39.414 1.00 36.37 OATOM 3033 C SER B 436 24.077 44.815 38.112 1.00 30.64 C ATOM 3034 O SERB 436 25.039 44.069 38.281 1.00 28.51 O ATOM 3035 N ASN B 437 22.83244.464 38.426 1.00 25.41 N ATOM 3036 CA ASN B 437 22.502 43.155 38.9931.00 26.86 C ATOM 3037 CB ASN B 437 21.088 43.219 39.581 1.00 29.47 CATOM 3038 CG ASN B 437 20.692 41.975 40.391 1.00 32.65 C ATOM 3039 OD1ASN B 437 19.669 41.997 41.081 1.00 33.91 O ATOM 3040 ND2 ASN B 43721.466 40.891 40.294 1.00 29.62 N ATOM 3041 C ASN B 437 22.632 42.12137.858 1.00 26.75 C ATOM 3042 O ASN B 437 23.126 41.010 38.070 1.0026.10 O ATOM 3043 N VAL B 438 22.220 42.483 36.648 1.00 26.29 N ATOM3044 CA VAL B 438 22.390 41.546 35.548 1.00 22.79 C ATOM 3045 CB VAL B438 21.761 42.073 34.250 1.00 26.63 C ATOM 3046 CG1 VAL B 438 22.08541.136 33.099 1.00 25.60 C ATOM 3047 CG2 VAL B 438 20.231 42.187 34.4281.00 27.00 C ATOM 3048 C VAL B 438 23.896 41.313 35.343 1.00 25.06 CATOM 3049 O VAL B 438 24.325 40.178 35.172 1.00 22.07 O ATOM 3050 N ALAB 439 24.704 42.383 35.376 1.00 23.57 N ATOM 3051 CA ALA B 439 26.15642.223 35.206 1.00 24.57 C ATOM 3052 CB ALA B 439 26.858 43.623 35.1351.00 23.14 C ATOM 3053 C ALA B 439 26.775 41.369 36.326 1.00 21.99 CATOM 3054 O ALA B 439 27.724 40.622 36.086 1.00 23.36 O ATOM 3055 N GLUB 440 26.225 41.467 37.540 1.00 22.47 N ATOM 3056 CA GLU B 440 26.72940.684 38.660 1.00 26.63 C ATOM 3057 CB GLU B 440 25.946 41.027 39.9371.00 28.89 C ATOM 3058 CG GLU B 440 26.220 40.080 41.109 1.00 27.35 CATOM 3059 CD GLU B 440 25.304 40.355 42.295 1.00 39.88 C ATOM 3060 OE1GLU B 440 24.142 40.766 42.075 1.00 37.76 O ATOM 3061 OE2 GLU B 44025.750 40.145 43.445 1.00 37.86 O ATOM 3062 C GLU B 440 26.575 39.19038.331 1.00 28.92 C ATOM 3063 O GLU B 440 27.503 38.411 38.506 1.0022.24 O ATOM 3064 N LEU B 441 25.393 38.812 37.848 1.00 22.17 N ATOM3065 CA LEU B 441 25.086 37.423 37.488 1.00 22.51 C ATOM 3066 CB LEU B441 23.590 37.301 37.148 1.00 22.22 C ATOM 3067 CG LEU B 441 22.64737.692 38.290 1.00 26.11 C ATOM 3068 CD1 LEU B 441 21.191 37.675 37.8231.00 26.08 C ATOM 3069 CD2 LEU B 441 22.853 36.702 39.443 1.00 23.20 CATOM 3070 C LEU B 441 25.930 36.973 36.296 1.00 20.83 C ATOM 3071 O LEUB 441 26.449 35.848 36.280 1.00 22.40 O ATOM 3072 N LEU B 442 26.06237.829 35.290 1.00 20.51 N ATOM 3073 CA LEU B 442 26.893 37.442 34.1471.00 24.46 C ATOM 3074 CB LEU B 442 26.822 38.487 33.038 1.00 22.94 CATOM 3075 CG LEU B 442 25.484 38.527 32.291 1.00 21.56 C ATOM 3076 CD1LEU B 442 25.459 39.693 31.263 1.00 24.52 C ATOM 3077 CD2 LEU B 44225.268 37.168 31.601 1.00 22.91 C ATOM 3078 C LEU B 442 28.346 37.24434.590 1.00 21.94 C ATOM 3079 O LEU B 442 29.033 36.352 34.105 1.0022.31 O ATOM 3080 N HIS B 443 28.811 38.055 35.530 1.00 20.83 N ATOM3081 CA HIS B 443 30.193 37.888 35.998 1.00 21.14 C ATOM 3002 CB HIS B443 30.598 39.048 36.918 1.00 25.52 C ATOM 3083 CG HIS B 443 31.96538.875 37.502 1.00 27.68 C ATOM 3084 CD2 HIS B 443 33.143 38.507 36.9321.00 25.68 C ATOM 3085 ND1 HIS B 443 32.210 38.987 38.855 1.00 26.29 NATOM 3086 CE1 HIS B 443 33.476 38.691 39.096 1.00 24.28 C ATOM 3087 NE2HIS B 443 34.064 38.394 37.947 1.00 23.65 N ATOM 3088 C HIS B 443 30.36736.530 36.715 1.00 22.96 C ATOM 3089 O HIS B 443 31.374 35.841 36.5411.00 21.47 O ATOM 3090 N GLN B 444 29.370 36.130 37.498 1.00 22.87 NATOM 3091 CA GLN B 444 29.429 34.843 38.177 1.00 19.38 C ATOM 3092 CBGLN B 444 28.203 34.688 39.080 1.00 21.91 C ATOM 3093 CG GLN B 44428.254 35.697 40.221 1.00 22.66 C ATOM 3094 CD GLN B 444 27.013 35.64841.058 1.00 25.66 C ATOM 3095 OE1 GLN B 444 25.994 35.130 40.633 1.0027.50 O ATOM 3096 NE2 GLN B 444 27.089 36.206 42.258 1.00 22.05 C ATOM3097 C GLN B 444 29.483 33.735 37.149 1.00 22.05 C ATOM 3098 O GLN B 44430.248 32.792 37.288 1.00 23.64 O ATOM 3099 N VAL B 445 28.691 33.86736.089 1.00 20.47 N ATOM 3100 CA VAL B 445 28.735 32.863 35.044 1.0019.55 C ATOM 3101 CB VAL B 445 27.705 33.147 33.926 1.00 20.65 C ATOM3102 CG1 VAL B 445 27.876 32.121 32.784 1.00 21.65 C ATOM 3103 CG2 VAL B445 26.300 33.049 34.493 1.00 21.06 C ATOM 3104 C VAL B 445 30.15132.857 34.435 1.00 21.63 C ATOM 3105 O VAL B 445 30.682 31.792 34.1501.00 21.53 O ATOM 3106 N SER B 446 30.757 34.031 34.251 1.00 19.30 NATOM 3107 CA SER B 446 32.108 34.047 33.663 1.00 22.00 C ATOM 3108 CBSER B 446 32.570 35.480 33.292 1.00 19.55 C ATOM 3109 OG SER B 44632.902 36.261 34.407 1.00 22.80 O ATOM 3110 C SER B 446 33.142 33.39934.600 1.00 22.37 C ATOM 3111 O SER B 446 34.109 32.812 34.131 1.0021.37 O ATOM 3112 N MET B 447 32.925 33.497 35.909 1.00 20.23 N ATOM3113 CA MET B 447 33.860 32.859 36.846 1.00 24.29 C ATOM 3114 CB MET B447 33.640 33.376 38.272 1.00 23.41 C ATOM 3115 CG MET B 447 34.12334.806 38.446 1.00 27.21 C ATOM 3116 SD MET B 447 34.087 35.327 40.2181.00 29.84 S ATOM 3117 CE MET B 447 32.347 35.711 40.421 1.00 28.71 CATOM 3118 C MET B 447 33.698 31.342 36.767 1.00 24.03 C ATOM 3119 O METB 447 34.681 30.617 36.778 1.00 23.04 O ATOM 3120 N GLY B 448 32.46030.858 36.669 1.00 19.35 N ATOM 3121 CA GLY B 448 32.276 29.423 36.5461.00 21.93 C ATOM 3122 C GLY B 448 32.898 28.922 35.248 1.00 28.63 CATOM 3123 O GLY B 448 33.506 27.847 35.242 1.00 23.12 O ATOM 3124 N METB 449 32.758 29.687 34.155 1.00 21.69 N ATOM 3125 CA MET B 449 33.32529.240 32.866 1.00 20.45 C ATOM 3126 CB MET B 449 32.714 30.027 31.6921.00 22.80 C ATOM 3127 CG MET B 449 31.201 29.789 31.468 1.00 21.04 CATOM 3128 SD MET B 449 30.734 28.035 31.300 1.00 25.98 S ATOM 3129 CEMET B 449 31.656 27.593 29.836 1.00 24.75 C ATOM 3130 C MET B 449 34.85229.343 32.825 1.00 19.20 C ATOM 3131 O MET B 449 35.526 28.532 32.1821.00 23.26 O ATOM 3132 N LYS B 450 35.399 30.330 33.520 1.00 21.31 NATOM 3133 CA LYS B 450 36.847 30.477 33.578 1.00 22.27 C ATOM 3134 CBLYS B 450 37.188 31.710 34.397 1.00 25.65 C ATOM 3135 CG LYS B 45038.686 31.870 34.602 1.00 35.16 C ATOM 3136 CD LYS B 450 38.967 32.94035.604 1.00 39.35 C ATOM 3137 CE LYS B 450 40.432 32.855 36.005 1.0041.39 C ATOM 3138 NZ LYS B 450 40.770 33.998 36.884 1.00 50.53 N ATOM3139 C LYS B 450 37.382 29.201 34.259 1.00 21.58 C ATOM 3140 O LYS B 45038.395 28.634 33.863 1.00 23.54 O ATOM 3141 N TYR B 451 36.667 28.73835.272 1.00 22.85 N ATOM 3142 CA TYR B 451 37.061 27.508 35.980 1.0026.56 C ATOM 3143 CB TYR B 451 36.179 27.307 37.225 1.00 31.08 C ATOM3144 CG TYR B 451 36.420 25.996 37.963 1.00 26.37 C ATOM 3145 CD1 TYR B451 37.523 25.831 38.813 1.00 32.42 C ATOM 3146 CE1 TYR B 451 37.71924.612 39.503 1.00 35.50 C ATOM 3147 CD2 TYR B 451 35.543 24.934 37.8101.00 29.25 C ATOM 3148 CE2 TYR B 451 35.737 23.731 39.458 1.00 36.41 CATOM 3149 CZ TYR B 451 36.814 23.570 39.307 1.00 36.89 C ATOM 3150 OHTYR B 451 36.928 22.357 39.947 1.00 35.03 O ATOM 3151 C TYR B 451 36.97526.290 35.084 1.00 23.27 O ATOM 3152 O TYR B 451 37.904 25.484 35.0351.00 22.89 O ATOM 3153 N LEU B 452 35.881 26.144 34.339 1.00 21.39 NATOM 3154 CA LEU B 452 35.757 25.005 33.457 1.00 21.19 C ATOM 3155 CBLEU B 452 34.379 24.995 32.735 1.00 25.34 C ATOM 3156 CG LEU B 45233.197 24.695 33.653 1.00 31.38 C ATOM 3157 CD1 LEU B 452 31.922 24.87232.832 1.00 39.34 C ATOM 3158 CD2 LEU B 452 33.275 23.271 34.196 1.0034.35 C ATOM 3159 C LEU B 452 36.855 24.995 32.417 1.00 23.04 C ATOM3160 O LEU B 452 37.399 23.390 32.098 1.00 23.98 O ATOM 3161 N GLU B 45337.178 26.179 31.894 1.00 21.93 N ATOM 3162 CA GLU B 453 38.215 26.29830.881 1.00 24.62 C ATOM 3163 CB GLU B 453 38.283 27.747 30.398 1.0025.46 C ATOM 3164 CG GLU B 453 39.415 28.050 29.406 1.00 28.82 C ATOM3165 CD GLU B 453 39.405 29.510 28.934 1.00 36.37 C ATOM 3166 OE1 GLU B453 40.016 30.376 29.621 1.00 33.79 O ATOM 3167 OE2 GLU B 453 38.77629.790 27.880 1.00 31.16 O ATOM 3168 C GLU B 453 39.585 25.865 31.4541.00 25.13 C ATOM 3169 O GLU B 453 40.345 25.115 30.812 1.00 25.39 OATOM 3170 N GLU B 454 39.908 26.351 32.645 1.00 22.62 N ATOM 3171 CA GLUB 454 41.204 25.996 33.245 1.00 26.22 C ATOM 3172 CB GLU B 454 41.43626.762 34.552 1.00 30.29 C ATOM 3173 CG GLU B 454 40.519 26.379 35.6811.00 43.54 C ATOM 3174 CD GLU B 454 40.821 27.144 36.972 1.00 58.22 CATOM 3175 OE1 GLU B 454 40.838 28.404 36.941 1.00 50.28 O ATOM 3176 OE2GLU B 454 41.029 26.480 38.019 1.00 56.54 O ATOM 3177 C GLU B 454 41.28424.501 33.507 1.00 32.56 C ATOM 3178 O GLU B 454 42.368 23.927 33.4891.00 31.49 O ATOM 3179 N LYS B 455 40.147 23.852 33.728 1.00 26.00 NATOM 3180 CA LYS B 455 40.141 22.406 33.979 1.00 27.14 C ATOM 3181 CBLYS B 455 39.043 22.032 34.991 1.00 26.60 C ATOM 3182 CG LYS B 45539.173 22.743 36.346 1.00 29.96 C ATOM 3183 CD LYS B 455 40.493 22.36537.009 1.00 36.01 C ATOM 3184 CE LYS B 455 40.733 23.118 38.322 1.0040.11 C ATOM 3185 NZ LYS B 455 42.067 22.747 38.909 1.00 33.10 N ATOM3186 C LYS B 455 39.954 21.605 32.692 1.00 26.89 C ATOM 3187 O LYS B 45539.757 20.397 32.732 1.00 31.85 O ATOM 3188 N ASN B 456 40.047 22.28031.551 1.00 27.82 N ATOM 3189 CA ASN B 456 39.901 21.640 30.245 1.0030.31 C ATOM 3190 CB ASN B 456 41.089 20.707 29.967 1.00 32.92 C ATOM3191 CG ASN B 456 42.384 21.456 29.907 1.00 40.95 C ATOM 3192 OD1 ASN B456 42.556 22.351 29.081 1.00 37.33 O ATOM 3193 ND2 ASN B 456 43.31321.110 30.803 1.00 43.15 N ATOM 3194 C ASN B 456 38.602 20.891 29.9921.00 30.21 C ATOM 3195 O ASN B 456 38.614 19.772 39.473 1.00 28.50 OATOM 3196 N PHE B 457 37.482 21.494 30.381 1.00 25.11 N ATOM 3197 CA PHEB 457 36.193 20.899 30.098 1.00 22.51 C ATOM 3198 CB PHE B 457 35.37620.679 31.386 1.00 23.31 C ATOM 3179 CG PHE B 457 35.848 19.515 32.2041.00 26.75 C ATOM 3200 CD1 PHE B 457 36.692 19.706 33.302 1.00 38.60 CATOM 3201 CD2 PHE B 457 35.456 18.232 31.877 1.00 29.58 C ATOM 3202 CE1PHE B 457 37.125 18.614 34.055 1.00 35.33 C ATOM 3203 CE2 PHE B 45735.887 17.140 32.624 1.00 29.78 C ATOM 3204 CZ PHE B 457 36.718 17.33433.710 1.00 29.78 C ATOM 3205 C PHE B 457 35.435 21.903 29.198 1.0020.08 C ATOM 3206 O PHE B 457 35.555 23.105 29.396 1.00 24.84 O ATOM3207 N VAL B 458 34.657 21.370 28.247 1.00 22.46 N ATOM 3208 CA VAL B458 33.832 22.189 27.351 1.00 19.50 C ATOM 3209 CB VAL B 458 34.03921.771 25.864 1.00 24.51 C ATOM 3210 CG1 VAL B 458 33.044 22.521 24.9461.00 20.39 C ATOM 3211 CG2 VAL B 458 35.451 22.094 25.438 1.00 26.69 CATOM 3212 C VAL B 458 32.365 21.908 27.749 1.00 22.31 C ATOM 3213 O VALB 458 31.956 20.779 27.818 1.00 23.69 O ATOM 3214 N HIS B 459 31.58122.946 27.977 1.00 21.21 N ATOM 3215 CA HIS B 459 30.176 22.720 28.4151.00 20.87 C ATOM 3216 CB HIS B 459 29.670 23.998 29.119 1.00 26.99 CATOM 3217 CG HIS B 459 28.294 23.866 29.693 1.00 26.79 C ATOM 3218 CD2HIS B 459 27.869 23.814 30.978 1.00 33.82 C ATOM 3219 ND1 HIS B 45927.163 23.762 28.912 1.00 30.62 N ATOM 3220 CE1 HIS B 459 26.099 23.66529.691 1.00 28.63 C ATOM 3221 NE2 HIS B 459 26.500 23.693 30.949 1.0026.47 N ATOM 3222 C HIS B 459 29.279 22.376 27.225 1.00 22.74 C ATOM3223 O HIS B 459 28.472 21.409 27.260 1.00 26.21 O ATOM 3224 N ARG B 46029.432 32.186 26.178 1.00 23.74 N ATOM 3225 CA ARG B 460 28.716 23.08324.911 1.00 23.96 C ATOM 3226 CB ARG B 460 28.766 21.644 24.390 1.0027.31 C ATOM 3227 CG ARG B 460 28.259 21.546 22.972 1.00 37.56 C ATOM3228 CD ARG B 460 28.279 20.147 22.427 1.00 32.14 C ATOM 3229 NE ARG B460 27.254 20.032 21.406 1.00 31.71 N ATOM 3230 CZ ARG B 460 27.00818.927 20.699 1.00 39.03 C ATOM 3231 NH1 ARG B 460 27.721 17.830 20.9031.00 34.17 N ATOM 3232 NH2 ARG B 460 26.040 18.924 19.793 1.00 42.19 NATOM 3233 C ARG B 460 27.261 23.562 24.895 1.00 30.30 C ATOM 3234 O ARGB 460 26.726 23.888 23.833 1.00 37.44 O ATOM 3235 N ASP B 461 26.62823.648 26.054 1.00 24.84 N ATOM 3236 CA ASP B 461 25.230 24.057 26.0871.00 27.22 C ATOM 3237 CB ASP B 461 24.389 22.843 26.547 1.00 29.93 CATOM 3238 CG ASP B 461 22.893 22.954 26.185 1.00 40.58 C ATOM 3239 OD1ASP B 461 22.497 23.822 25.374 1.00 47.29 O ATOM 3240 OD2 ASP B 46122.100 22.138 26.718 1.00 51.22 O ATOM 3241 C ASP B 461 25.039 25.28126.998 1.00 27.48 C ATOM 3242 O ASP B 461 24.054 25.401 27.713 1.0025.86 O ATOM 3243 N LEU B 462 25.985 26.210 26.963 1.00 21.15 N ATOM3244 CA LEU B 462 25.841 27.339 27.788 1.00 20.41 C ATOM 3245 CB LEU B462 27.200 28.106 27.940 1.00 22.91 C ATOM 3246 CG LEU B 462 27.21629.380 28.792 1.00 28.71 C ATOM 3247 CD1 LEU B 462 26.774 29.008 30.2031.00 30.96 C ATOM 3248 CD2 LEU B 462 28.614 30.037 28.792 1.00 27.89 CATOM 3249 C LEU B 462 24.790 28.300 27.113 1.00 25.32 C ATOM 3250 O LEUB 462 24.913 28.640 25.958 1.00 27.45 O ATOM 3251 N ALA B 463 23.73728.637 27.847 1.00 20.92 N ATOM 3252 CA ALA B 463 22.645 29.482 27.3501.00 20.29 C ATOM 3253 CB ALA B 463 21.709 28.658 26.431 1.00 17.73 CATOM 3254 C ALA B 463 21.905 29.962 28.596 1.00 21.81 C ATOM 3255 O ALAB 463 21.978 29.319 29.655 1.00 21.64 O ATOM 3256 N ALA B 464 21.18731.069 28.492 1.00 19.40 N ATOM 3257 CA ALA B 464 20.510 31.586 29.6551.00 21.46 C ATOM 3258 CB ALA B 464 19.750 32.879 29.294 1.00 20.54 CATOM 3259 C ALA B 464 19.567 30.560 30.288 1.00 23.11 C ATOM 3260 O ALAB 464 19.399 30.567 31.499 1.00 22.21 O ATOM 3261 N ARG B 465 18.96329.703 29.468 1.00 22.19 N ATOM 3262 CA ARG B 465 18.036 28.679 29.9551.00 25.34 C ATOM 3263 CB ARG B 465 17.372 27.947 28.783 1.00 22.79 CATOM 3264 CG ARG B 465 18.310 27.131 27.897 1.00 21.09 C ATOM 3265 CDARG B 465 17.586 26.576 26.650 1.00 28.36 C ATOM 3266 NE ARG B 46518.537 25.936 25.752 1.00 33.20 N ATOM 3267 CZ ARG B 465 19.230 26.56824.801 1.00 41.11 C ATOM 3268 NH1 ARG B 465 19.074 27.873 24.592 1.0034.56 N ATOM 3269 NH2 ARG B 465 20.129 25.908 24.099 1.00 36.89 N ATOM3270 C ARG B 465 18.746 27.650 30.840 1.00 27.21 C ATOM 3271 O ARG B 46518.098 26.930 31.600 1.00 25.31 O ATOM 3272 N ASN B 466 20.075 27.58330.727 1.00 26.22 N ATOM 3273 CA ASN B 466 20.851 26.640 31.535 1.0022.74 C ATOM 3274 CB ASN B 466 21.777 25.809 30.647 1.00 20.44 C ATOM3275 CG ASN B 466 21.022 24.810 29.806 1.00 31.49 C ATOM 3276 OD1 ASN B466 19.963 34.316 30.217 1.00 26.09 O ATOM 3277 ND2 ASN B 466 21.55624.496 28.624 1.00 25.81 N ATOM 3278 C ASN B 466 21.608 27.277 32.6771.00 24.14 C ATOM 3279 O ASN B 466 22.379 26.617 33.372 1.00 25.61 OATOM 3280 N VAL B 467 21.384 28.563 32.895 1.00 19.90 N ATOM 3281 CA VALB 467 21.999 29.239 34.013 1.00 18.65 C ATOM 3282 CB VAL B 467 22.44330.652 33.640 1.00 21.94 C ATOM 3283 CG1 VAL B 467 22.840 31.414 34.9101.00 20.29 C ATOM 3284 CG2 VAL B 467 23.617 31.414 32.634 1.00 21.43 CATOM 3285 C VAL B 467 20.834 29.323 35.002 1.00 25.03 C ATOM 3286 O VALB 467 19.757 29.829 34.659 1.00 24.55 O ATOM 3287 N LEU B 468 21.04728.821 36.212 1.00 21.56 N ATOM 3288 CA LEU B 468 19.972 28.813 37.2191.00 22.81 C ATOM 3289 CB LEU B 468 19.738 27.385 37.734 1.00 22.41 CATOM 3290 CG LEU B 468 19.493 26.291 36.695 1.00 25.80 C ATOM 3291 CD1LEU B 468 19.568 24.927 37.347 1.00 27.13 C ATOM 3292 CD2 LEU B 46818.128 26.521 36.038 1.00 28.96 C ATOM 3293 C LEU B 468 20.287 29.70738.394 1.00 27.22 C ATOM 3294 O LEU B 468 21.426 29.782 38.826 1.0026.70 O ATOM 3295 N LEU B 469 19.262 30.349 38.960 1.00 24.32 N ATOM3296 CA LEU B 469 19.511 31.234 40.078 1.00 23.08 C ATOM 3297 CB LEU B469 18.687 32.498 39.908 1.00 24.42 C ATOM 3298 CG LEU B 469 18.98533.232 38.596 1.00 37.62 C ATOM 3299 CD1 LEU B 469 17.999 34.336 38.4121.00 40.80 C ATOM 3300 CD2 LEU B 469 20.384 33.797 38.612 1.00 33.91 CATOM 3301 C LEU B 469 19.216 30.625 41.440 1.00 26.89 C ATOM 3302 O LEUB 469 18.162 30.024 41.643 1.00 27.22 O ATOM 3303 N VAL B 470 20.15430.766 42.366 1.00 27.63 N ATOM 3304 CA VAL B 470 19.903 30.311 43.7181.00 30.31 C ATOM 3305 CB VAL B 470 21.199 30.132 44.520 1.00 33.68 CATOM 3306 CG1 VAL B 470 20.862 29.797 45.973 1.00 34.34 C ATOM 3307 CG2VAL B 470 22.027 29.002 43.912 1.00 28.72 C ATOM 3308 C VAL B 470 19.05731.450 44.300 1.00 31.84 C ATOM 3309 O VAL B 470 18.096 31.210 45.0511.00 33.69 O ATOM 3310 N ASN B 471 19.407 36.682 43.930 1.00 29.94 NATOM 3311 CA ASN B 471 18.688 33.903 44.335 1.00 34.01 C ATOM 3312 CBASN B 471 19.139 34.394 45.723 1.00 38.51 C ATOM 3313 CG ASN B 47120.631 34.554 45.824 1.00 41.61 C ATOM 3314 OD1 ASN B 471 21.336 33.62746.225 1.00 62.13 O ATOM 3315 ND2 ASN B 471 21.129 35.710 45.433 1.0034.16 N ATOM 3316 C ASN B 471 19.009 34.971 43.283 1.00 32.05 C ATOM3317 O ASN B 471 19.796 34.712 42.378 1.00 29.59 O ATOM 3318 N ARG B 47218.434 36.170 43.395 1.00 31.13 N ATOM 3319 CA ARG B 472 18.687 37.21642.392 1.00 33.64 C ATOM 3320 CB ARG B 472 17.766 38.417 42.631 1.0035.84 C ATOM 3321 CG ARG B 472 18.042 39.147 43.924 1.00 37.87 C ATOM3322 CD ARG B 472 17.142 40.371 44.053 1.00 40.99 C ATOM 3323 NE ARG B472 17.621 41.483 43.240 1.00 43.11 N ATOM 3324 CZ ARG B 472 16.97242.633 43.074 1.00 48.70 C ATOM 3325 NH1 ARG B 472 15.795 42.832 43.6671.00 41.99 N ATOM 3326 NH2 ARG B 472 17.503 43.593 42.334 1.00 44.48 NATOM 3327 C ARG B 472 20.132 37.702 42.324 1.00 24.49 C ATOM 3328 O ARGB 472 20.492 38.446 41.423 1.00 30.50 O ATOM 3329 N HIS B 473 20.95237.294 43.288 1.00 26.54 N ATOM 3330 CA HIS B 473 22.340 37.700 43.3241.00 30.93 C ATOM 3331 CB HIS B 473 22.628 38.717 44.614 1.00 28.14 CATOM 3332 CG HIS B 473 21.888 39.817 44.673 1.00 32.49 C ATOM 3333 CD2HIS B 473 20.856 40.225 45.451 1.00 40.34 C ATOM 3334 ND1 HIS B 47322.125 40.845 43.786 1.00 36.03 N ATOM 3335 CE1 HIS B 473 21.266 41.82544.008 1.00 41.10 C ATOM 3336 NE2 HIS B 473 20.482 41.473 45.013 1.0042.57 N ATOM 3337 C HIS B 473 23.276 36.497 43.260 1.00 25.86 C ATOM3338 O HIS B 473 24.472 36.628 43.573 1.00 25.18 O ATOM 3339 N TYR B 47422.760 35.337 42.854 1.00 26.93 N ATOM 3340 CA TYR B 474 23.614 34.14142.810 1.00 28.61 C ATOM 3341 CB TYR B 474 23.597 33.447 44.184 1.0026.00 C ATOM 3342 CG TYR B 474 24.589 32.302 44.396 1.00 29.87 C ATOM3343 CD1 TYR B 474 25.645 32.050 43.505 1.00 27.42 C ATOM 3344 CE1 TYR B474 26.563 30.995 43.747 1.00 31.28 C ATOM 3345 CD2 TYR B 474 24.47731.481 45.523 1.00 34.24 C ATOM 3346 CE2 TYR B 474 25.377 30.444 45.7681.00 37.06 C ATOM 3347 CZ TYR B 474 26.416 30.198 44.888 1.00 35.99 CATOM 3348 OH TYR B 474 27.285 29.160 45.187 1.00 32.29 O ATOM 3349 C TYRB 474 23.218 33.160 41.719 1.00 27.49 C ATOM 3350 O TYR B 474 22.23732.413 41.862 1.00 27.72 O ATOM 3351 N ALA B 475 24.003 33.153 40.6381.00 21.66 N ATOM 3352 CA ALA B 475 23.744 32.279 39.509 1.00 25.73 CATOM 3353 CB ALA B 475 23.886 33.075 38.200 1.00 27.00 C ATOM 3354 C ALAB 475 24.680 31.057 39.486 1.00 25.53 C ATOM 3355 O ALA B 475 25.80931.113 39.970 1.00 26.97 0 ATOM 3356 N LYS B 476 24.190 29.953 38.9211.00 22.58 N ATOM 3357 CA LYS B 476 24.987 28.739 38.771 1.00 23.46 CATOM 3358 CB LYS B 476 24.594 27.691 39.834 1.00 24.43 C ATOM 3359 CGLYS B 476 25.144 28.000 41.221 1.00 25.55 C ATOM 3360 CD LYS B 47624.578 26.972 42.233 1.00 32.01 C ATOM 3361 CE LYS B 476 25.288 27.03643.577 1.00 36.59 C ATOM 3362 NZ LYS B 476 26.553 26.248 43.526 1.0037.14 N ATOM 3363 C LYS B 476 24.787 28.124 37.402 1.00 24.32 C ATOM3364 O LYS B 476 23.658 28.084 36.876 1.00 24.88 O ATOM 3365 N ILE B 47725.869 27.620 36.815 1.00 21.48 N ATOM 3366 CA ILE B 477 25.778 26.98035.511 1.00 23.09 C ATOM 3367 CB ILE B 477 27.139 26.937 34.843 1.0020.87 C ATOM 3368 CG2 ILE B 477 27.065 26.129 33.544 1.00 24.48 C ATOM3369 CG1 ILE B 477 27.644 28.370 34.642 1.00 22.01 C ATOM 3370 CD1 ILE B477 29.143 28.461 34.443 1.00 23.58 C ATOM 3371 C ILE B 477 25.29725.560 35.689 1.00 26.88 C ATOM 3372 O ILE B 477 25.794 24.860 36.5651.00 24.82 O ATOM 3373 N SER B 478 24.351 25.111 34.855 1.00 22.63 NATOM 3374 CA SER B 478 23.876 23.743 34.992 1.00 23.59 C ATOM 3375 CBSER B 478 22.474 23.741 35.578 1.00 30.50 C ATOM 3376 OG SER B 47821.607 24.274 34.601 1.00 40.13 O ATOM 3377 C SER B 478 23.842 22.99633.664 1.00 27.84 C ATOM 3378 O SER B 478 24.253 23.528 32.616 1.0027.42 O ATOM 3379 N ASP B 479 23.302 21.775 33.730 1.00 23.72 N ATOM3380 CA ASP B 479 23.164 20.821 32.611 1.00 25.82 C ATOM 3381 CB ASP B479 22.094 21.256 31.585 1.00 24.35 C ATOM 3382 CG ASP B 479 21.71120.104 30.636 1.00 34.90 C ATOM 3383 OD1 ASP B 479 22.419 19.076 30.6361.00 30.23 O ATOM 3384 OD2 ASP B 479 20.703 20.214 29.899 1.00 30.91 OATOM 3385 C ASP B 479 24.460 20.489 31.878 1.00 24.50 C ATOM 3386 O ASPB 479 24.751 21.037 30.784 1.00 21.34 O ATOM 3387 N PHE B 480 25.19719.529 32.444 1.00 26.62 N ATOM 3388 CA PHE B 480 26.464 19.062 31.8631.00 27.44 C ATOM 3389 CB PHE B 480 27.474 18.812 32.993 1.00 26.01 CATOM 3390 CG PHE B 480 27.893 20.075 33.696 1.00 25.53 C ATOM 3391 CD1PHE B 480 29.029 20.788 33.289 1.00 37.11 C ATOM 3392 CD2 PHE B 48027.095 20.617 34.700 1.00 30.32 C ATOM 3393 CE1 PHE B 480 29.346 22.02333.870 1.00 34.94 C ATOM 3394 CE2 PHE B 480 27.403 21.850 35.279 1.0031.64 C ATOM 3395 CZ PHE B 480 28.520 22.555 34.866 1.00 33.32 C ATOM3396 C PHE B 480 26.288 17.810 30.989 1.00 23.32 C ATOM 3397 O PHE B 48027.242 17.078 30.712 1.00 29.60 O ATOM 3398 N GLY B 481 25.059 17.58630.533 1.00 24.87 N ATOM 3399 CA GLY B 481 24.743 16.444 29.690 1.0025.16 C ATOM 3400 C GLY B 481 25.510 16.367 28.377 1.00 32.36 C ATOM3401 O GLY B 481 25.643 15.300 27.819 1.00 28.44 O ATOM 3402 N LEU B 48226.017 17.491 27.876 1.00 24.22 N ATOM 3403 CA LEU B 482 26.778 17.47426.617 1.00 24.32 C ATOM 3404 CB LEU B 482 26.169 18.473 25.622 1.0027.61 C ATOM 3405 CG LEU B 482 24.767 18.111 25.133 1.00 31.09 C ATOM3406 CD1 LEU B 482 24.143 19.316 24.392 1.00 37.33 C ATOM 3407 CD2 LEU B482 24.868 16.912 24.231 1.00 33.44 C ATOM 3408 C LEU B 482 28.29917.843 26.833 1.00 20.28 C ATOM 3409 O LEU B 482 28.998 18.006 25.8811.00 27.53 O ATOM 3410 N SER B 483 28.607 17.986 28.093 1.00 21.03 NATOM 3411 CA SER B 483 29.959 18.392 28.423 1.00 17.07 C ATOM 3412 CBSER B 483 30.001 18.818 29.882 1.00 21.12 C ATOM 3413 OG SER B 48329.143 19.933 30.053 1.00 31.09 O ATOM 3414 C SER B 483 30.984 17.29828.156 1.00 21.12 C ATOM 3415 O SER B 483 30.662 16.131 28.176 1.0023.30 O ATOM 3416 N LYS B 484 32.225 17.700 27.901 1.00 22.23 N ATOM3417 CA LYS B 484 33.281 16.732 27.641 1.00 22.46 C ATOM 3418 CB LYS B484 33.403 16.456 26.135 1.00 25.43 C ATOM 3419 CG LYS B 484 32.20215.661 25.564 1.00 37.37 C ATOM 3420 CD LYS B 484 32.323 15.382 24.0691.00 42.87 C ATOM 3421 CE LYS B 484 31.228 14.402 23.622 1.00 42.01 CATOM 3422 NZ LYS B 484 29.878 14.732 24.149 1.00 57.01 N ATOM 3423 C LYSB 484 34.622 17.227 28.157 1.00 26.66 C ATOM 3424 O LYS B 484 24.87018.426 28.229 1.00 25.66 O ATOM 3425 N ALA B 485 35.489 16.280 28.4921.00 22.91 N ATOM 3426 CA ALA B 485 36.825 16.636 28.962 1.00 21.91 CATOM 3427 CB ALA B 485 37.359 15.560 29.932 1.00 32.95 C ATOM 3428 C ALAB 485 37.689 16.684 27.679 1.00 29.52 C ATOM 3429 O ALA B 485 37.55215.827 26.804 1.00 32.44 O ATOM 3430 N LEU B 486 38.546 17.694 27.5761.00 24.43 N ATOM 3431 CA LEU B 486 39.419 17.841 26.403 1.00 19.74 CATOM 3432 CB LEU B 486 39.663 19.335 26.108 1.00 28.91 C ATOM 3433 CGLEU B 486 38.582 20.155 25.390 1.00 28.77 C ATOM 3434 CD1 LEU B 48638.967 21.633 25.366 1.00 34.39 C ATOM 3435 CD2 LEU B 486 38.408 19.62924.006 1.00 36.84 C ATOM 3436 C LEU B 486 40.794 17.187 26.636 1.0031.66 C ATOM 3437 O LEU B 486 41.477 16.831 25.690 1.00 34.07 O ATOM3438 N GLY B 487 41.203 17.066 27.897 1.00 30.25 N ATOM 3439 CA GLY B487 42.510 16.493 28.177 1.00 35.90 C ATOM 3440 C GLY B 487 43.59117.425 27.643 1.00 35.05 C ATOM 3441 O GLY B 487 43.547 18.624 27.8471.00 37.70 O ATOM 3442 N ALA B 488 44.540 16.853 26.919 1.00 36.40 NATOM 3443 CA ALA B 488 45.644 17.630 26.364 1.00 41.44 C ATOM 3444 CBALA B 488 46.841 16.711 26.100 1.00 44.00 C ATOM 3445 C ALA B 488 45.28318.375 25.080 1.00 40.64 C ATOM 3446 O ALA B 488 46.035 19.227 24.6271.00 40.65 O ATOM 3447 N ASP B 489 44.125 18.068 24.506 1.00 37.22 NATOM 3448 CA ASP B 489 43.706 18.723 23.255 1.00 35.43 C ATOM 3449 CBASP B 489 42.740 17.811 22.497 1.00 36.96 C ATOM 3450 CG ASP B 48943.331 16.450 22.240 1.00 48.65 C ATOM 3451 OD1 ASP B 489 44.563 16.38322.017 1.00 51.66 O ATOM 3452 OD2 ASP B 489 42.571 15.457 22.249 1.0047.30 O ATOM 3453 C ASP B 489 43.062 20.090 23.440 1.00 31.19 C ATOM3454 O ASP B 489 42.545 20.391 24.502 1.00 31.54 O ATOM 3455 N ASP B 49043.085 20.911 22.387 1.00 28.93 N ATOM 3456 CA ASP B 490 42.480 22.23522.480 1.00 31.45 C ATOM 3457 CB ASP B 490 43.333 23.272 21.742 1.0036.63 C ATOM 3458 CG ASP B 490 43.495 22.950 20.292 1.00 47.74 C ATOM3459 OD1 ASP B 490 44.554 23.298 19.706 1.00 55.99 O ATOM 3460 OD2 ASP B490 42.557 22.364 19.727 1.00 54.77 O ATOM 3461 C ASP B 490 41.04722.241 21.942 1.00 26.58 C ATOM 3462 O ASP B 490 40.347 23.252 22.0281.00 25.36 O ATOM 3463 N SER B 491 40.599 21.115 21.398 1.00 24.18 NATOM 3464 CA SER B 491 39.215 21.008 20.901 1.00 21.95 C ATOM 3465 CBSER B 491 39.067 21.782 19.592 1.00 33.37 C ATOM 3466 OG SER B 49139.830 21.147 18.559 1.00 33.09 O ATOM 3467 C SER B 491 38.879 19.57420.619 1.00 29.49 C ATOM 3468 O SER B 491 39.754 18.698 20.726 1.0026.31 O ATOM 3469 N TYR B 492 37.611 19.310 20.296 1.00 23.30 N ATOM3470 CA TYR B 492 37.228 17.987 19.891 1.00 24.79 C ATOM 3471 CB TYR B492 36.708 17.112 21.060 1.00 24.52 C ATOM 3472 CG TYR B 492 35.35817.507 21.590 1.00 26.67 C ATOM 3473 CD1 TYR B 492 34.187 16.946 21.0701.00 26.01 C ATOM 3474 CE1 TYR B 492 32.928 17.362 21.510 1.00 29.14 CATOM 3475 CD2 TYR B 492 35.249 18.487 22.568 1.00 24.91 C ATOM 3476 CE2TYR B 492 33.979 18.912 23.025 1.00 24.00 C ATOM 3477 CZ TYR B 49232.835 18.343 22.483 1.00 26.42 C ATOM 3478 OH TYR B 492 31.589 18.77522.887 1.00 26.61 O ATOM 3479 C TYR B 492 36.180 18.166 18.803 1.0020.40 C ATOM 3480 O TYR B 492 35.632 19.255 18.622 1.00 22.94 O ATOM3481 N TYR B 493 35.960 17.099 18.050 1.00 20.88 N ATOM 3482 CA TYR B493 34.958 17.072 16.980 1.00 19.63 C ATOM 3483 CB TYR B 493 35.55916.596 15.671 1.00 21.26 C ATOM 3484 CG TYR B 493 36.515 17.601 15.0951.00 24.50 C ATOM 3485 CD1 TYR B 493 37.777 17.769 15.645 1.00 27.04 CATOM 3486 CE1 TYR B 493 38.652 18.713 15.144 1.00 36.13 C ATOM 3487 CD2TYR B 493 36.137 18.407 14.014 1.00 26.33 C ATOM 3488 CE2 TYR B 49337.011 19.352 13.501 1.00 27.99 C ATOM 3489 CZ TYR B 493 38.262 19.49714.067 1.00 32.35 C ATOM 3490 OH TYR B 493 39.144 20.396 13.526 1.0033.44 O ATOM 3491 C TYR B 493 33.944 16.069 17.468 1.00 21.80 C ATOM3492 O TYR B 493 34.293 14.925 17.800 1.00 22.36 O ATOM 3493 N THR B 49432.695 16.514 17.539 1.00 26.46 N ATOM 3494 CA THR B 494 31.623 15.70018.095 1.00 33.93 C ATOM 3495 CB THR B 494 30.580 16.611 18.817 1.0033.02 C ATOM 3496 OG1 THR B 494 29.647 15.794 19.538 1.00 40.25 O ATOM3497 CG2 THR B 494 29.817 17.435 17.812 1.00 33.65 C ATOM 3498 C THR B494 30.875 14.851 17.104 1.00 36.70 C ATOM 3499 O THR B 494 30.75715.179 15.921 1.00 28.58 O ATOM 3500 N ALA B 495 30.294 13.773 17.6111.00 44.45 N ATOM 3501 CA ALA B 495 29.508 12.911 16.764 1.00 49.14 CATOM 3502 CB ALA B 495 29.442 11.529 17.370 1.00 47.66 C ATOM 3503 C ALAB 495 28.108 13.503 16.624 1.00 49.65 C ATOM 3504 O ALA B 495 27.65114.233 17.498 1.00 48.99 O ATOM 3505 N ARG B 496 27.446 13.194 15.5191.00 53.97 N ATOM 3506 CA ARG B 496 26.098 13.678 15.264 1.00 57.66 CATOM 3507 CB ARG B 496 25.804 13.674 13.759 1.00 60.80 C ATOM 3508 CGARG B 496 25.116 14.929 13.230 1.00 65.91 C ATOM 3509 CD ARG B 49623.905 15.299 14.043 1.00 66.81 C ATOM 3510 NE ARG B 496 23.322 16.55213.573 1.00 66.60 N ATOM 3511 CZ ARG B 496 22.295 17.160 14.156 1.0071.04 C ATOM 3512 NH1 ARG B 496 21.737 16.626 15.237 1.00 70.95 N ATOM3513 NH2 ARG B 496 21.826 18.299 13.660 1.00 66.70 N ATOM 3514 C ARG B496 25.106 12.741 15.964 1.00 60.28 C ATOM 3515 O ARG B 496 25.18511.519 15.826 1.00 58.20 O ATOM 3516 N SER B 497 24.183 13.316 16.7211.00 58.58 N ATOM 3517 CA SER B 497 23.175 12.513 17.407 1.00 60.66 CATOM 3518 CB SER B 497 23.267 12.711 18.920 1.00 58.31 C ATOM 3519 OGSER B 497 22.882 14.026 19.276 1.00 66.25 O ATOM 3520 C SER B 497 21.80912.965 16.913 1.00 60.66 C ATOM 3521 O SER B 497 21.711 13.896 16.1141.00 59.92 O ATOM 3522 N ALA B 498 20.764 12.305 17.396 1.00 63.28 NATOM 3523 CA ALA B 498 19.399 12.645 17.015 1.00 61.54 C ATOM 3524 CBALA B 498 18.440 11.531 17.450 1.00 58.15 C ATOM 3525 C ALA B 498 18.99513.963 17.671 1.00 60.15 C ATOM 3526 G ALA B 498 19.422 14.275 18.7831.00 59.70 O ATOM 3527 N GLY B 499 18.168 14.733 16.977 1.00 61.09 NATOM 3528 CA GLY B 499 17.719 15.994 17.533 1.00 63.27 C ATOM 3529 C GLYB 499 18.325 17.184 16.826 1.00 61.70 C ATOM 3530 O GLY B 499 19.30917.051 16.096 1.00 63.96 O ATOM 3531 N LYS B 500 17.735 18.352 17.0421.00 59.76 N ATOM 3532 CA LYS B 500 18.216 19.576 16.417 1.00 57.53 CATOM 3533 CB LYS B 500 17.052 20.550 16.210 1.00 60.45 C ATOM 3534 CGLYS B 500 16.017 20.091 15.199 1.00 61.48 C ATOM 3535 CD LYS B 50016.561 20.185 13.780 1.00 65.74 C ATOM 3536 CE LYS B 500 15.500 19.80012.756 1.00 62.41 C ATOM 3537 NZ LYS B 500 16.013 19.898 11.358 1.0067.47 N ATOM 3538 C LYS B 500 19.283 20.251 17.275 1.00 51.49 C ATOM3539 O LYS B 500 19.282 20.137 18.495 1.00 49.86 O ATOM 3540 N TRP B 50120.195 20.957 16.618 1.00 45.23 N ATOM 3541 CA TRP B 501 21.253 21.68017.325 1.00 46.44 C ATOM 3542 CB TRP B 501 22.530 21.673 16.483 1.0040.73 C ATOM 3543 CG TRP B 501 23.332 20.423 16.584 1.00 38.73 C ATOM3544 CD2 TRP B 501 24.704 20.258 16.199 1.00 35.99 C ATOM 3545 CE2 TRP B501 25.085 18.943 16.562 1.00 39.61 C ATOM 3546 CE3 TRP B 501 25.65121.095 15.586 1.00 39.41 C ATOM 3547 CD1 TRP B 501 22.942 19.235 17.1331.00 40.88 C ATOM 3548 NE1 TRP B 501 23.992 18.339 17.130 1.00 40.09 NATOM 3549 CZ3 TRP B 501 26.375 18.448 16.337 1.00 35.77 C ATOM 3550 CZ3TRP B 501 26.942 20.597 15.361 1.00 34.28 C ATOM 3551 CH2 TRP B 50127.286 19.287 15.739 1.00 40.15 C ATOM 3552 C TRP B 501 20.795 23.12617.545 1.00 39.13 C ATOM 3553 O TRP B 501 20.193 23.722 16.648 1.0042.06 O ATOM 3554 N PRO B 502 21.060 23.703 18.736 1.00 35.62 N ATOM3555 CD PRO B 502 21.732 23.060 19.884 1.00 36.26 C ATOM 3556 CA PRO B502 20.675 25.094 19.056 1.00 38.57 C ATOM 3557 CB PRO B 502 20.84125.158 20.569 1.00 36.44 C ATOM 3558 CG PRO B 502 22.021 24.232 20.8031.00 42.17 C ATOM 3559 C PRO B 502 21.650 26.019 18.328 1.00 34.08 CATOM 3560 O PRO B 502 22.528 26.650 18.941 1.00 27.50 O ATOM 3561 N LEUB 503 21.487 26.069 17.011 1.00 27.87 N ATOM 3562 CA LEU B 503 22.37726.847 16.147 1.00 30.99 C ATOM 3563 CB LEU B 503 21.846 26.834 14.7061.00 35.93 C ATOM 3564 CG LEU B 503 21.555 25.457 14.117 1.00 38.86 CATOM 3565 CD1 LEU B 503 20.943 25.607 12.720 1.00 46.43 C ATOM 3566 CD2LEU B 503 22.833 24.656 14.046 1.00 42.19 C ATOM 3567 C LEU B 503 22.60328.287 16.564 1.00 24.64 C ATOM 3568 O LEU B 503 23.707 28.826 16.3641.00 24.20 O ATOM 3569 N LYS B 504 21.586 28.914 17.154 1.00 24.76 NATOM 3570 CA LYS B 504 21.712 30.313 17.542 1.00 26.03 C ATOM 3571 CBLYS B 504 20.353 30.890 17.939 1.00 29.28 C ATOM 3572 CG LYS B 50419.400 31.000 16.729 1.00 31.16 C ATOM 3573 CD LYS B 504 18.070 31.65617.108 1.00 33.06 C ATOM 3574 CE LYS B 504 17.121 31.755 15.913 1.0034.32 C ATOM 3575 NZ LYS B 504 15.941 32.606 16.264 1.00 37.82 N ATOM3576 C LYS B 504 22.726 30.522 18.657 1.00 28.80 C ATOM 3577 O LYS B 50423.130 31.663 18.884 1.00 20.01 O ATOM 3578 N TRP B 505 23.141 29.49719.338 1.00 23.22 N ATOM 3579 CA TRP B 505 24.134 29.656 20.408 1.0019.35 C ATOM 3580 CB TRP B 505 23.681 28.883 21.665 1.00 25.81 C ATOM3581 CG TRP B 505 22.680 29.620 22.472 1.00 24.36 C ATOM 3582 CD2 TRP B505 21.277 29.724 22.215 1.00 22.43 C ATOM 3583 CE2 TRP B 505 20.73930.586 23.194 1.00 23.82 C ATOM 3584 CE3 TRP B 505 20.415 30.389 21.2511.00 27.42 C ATOM 3585 CD1 TRP B 505 22.934 30.389 23.567 1.00 18.37 CATOM 3586 NE1 TRP B 505 21.771 30.980 24.005 1.00 23.48 N ATOM 3587 CZ2TRP B 505 19.371 30.916 23.245 1.00 31.39 C ATOM 3588 CZ3 TRP B 50519.051 29.496 21.299 1.00 28.93 C ATOM 3589 CH2 TRP B 505 18.547 30.36522.296 1.00 25.25 C ATOM 3590 C TRP B 505 25.497 29.098 19.954 1.0019.69 C ATOM 3591 O TRP B 505 26.496 29.233 20.663 1.00 22.22 O ATOM3592 N TYR B 506 25.546 28.513 18.767 1.00 21.76 N ATOM 3593 CA TYR B506 26.794 27.885 18.285 1.00 22.94 C ATOM 3594 CB TYR B 506 26.42626.615 17.488 1.00 21.82 C ATOM 3595 CG TYR B 506 26.093 25.389 18.3391.00 23.08 C ATOM 3596 CD1 TYR B 506 25.885 25.496 19.710 1.00 25.11 CATOM 3597 CE1 TYR B 506 25.559 24.358 20.489 1.00 34.90 C ATOM 3598 CD2TYR B 506 25.981 24.124 17.751 1.00 29.64 C ATOM 3599 CE2 TYR B 50625.669 22.993 18.524 1.00 32.44 C ATOM 3600 CZ TYR B 506 25.454 23.11719.880 1.00 32.19 C ATOM 3601 OH TYR B 506 25.086 22.008 20.619 1.0037.37 O ATOM 3602 C TYR B 506 27.745 28.757 17.434 1.00 28.60 C ATOM3603 O TYR B 506 27.299 29.447 16.524 1.00 25.58 O ATOM 3604 N ALA B 50729.048 28.703 17.731 1.00 23.48 N ATOM 3605 CA ALA B 507 30.061 29.44016.980 1.00 22.63 C ATOM 3606 CB ALA B 507 31.443 29.298 17.674 1.0019.24 C ATOM 3607 C ALA B 507 30.122 28.845 15.567 1.00 24.54 C ATOM3608 O ALA B 507 29.709 27.709 15.343 1.00 23.92 O ATOM 3609 N PRO B 50830.659 29.597 14.603 1.00 22.52 N ATOM 3610 CD PRO B 508 31.136 30.98514.747 1.00 24.20 C ATOM 3611 CA PRO B 508 30.772 29.135 13.212 1.0023.99 C ATOM 3612 CB PRO B 508 31.546 30.265 12.529 1.00 28.71 C ATOM3613 CG PRO B 508 31.113 31.477 13.328 1.00 35.43 C ATOM 3614 C PRO B508 31.452 27.787 13.007 1.00 23.80 C ATOM 3615 O PRO B 508 30.96026.964 12.231 1.00 23.69 O ATOM 3616 N GLU B 509 32.576 27.568 13.6951.00 22.83 N ATOM 3617 CA GLU B 509 33.316 26.315 13.564 1.00 26.16 CATOM 3618 CB GLU B 509 34.689 26.390 14.268 1.00 26.11 C ATOM 3619 CGGLU B 509 34.622 26.429 15.792 1.00 25.28 C ATOM 3620 CD GLU B 50934.538 27.843 16.341 1.00 30.45 C ATOM 3621 OE1 GLU B 509 34.270 28.79815.561 1.00 24.15 O ATOM 3622 OE2 GLU B 509 34.716 27.989 17.568 1.0025.31 O ATOM 3623 C GLU B 509 32.512 25.128 14.098 1.00 22.82 C ATOM3624 O GLU B 509 32.751 23.992 13.686 1.00 25.61 O ATOM 3625 N CYS B 51031.571 25.389 15.010 1.00 20.67 N ATOM 3626 CA CYS B 510 30.726 24.32315.536 1.00 17.87 C ATOM 3627 CB CYS B 510 29.867 24.838 16.704 1.0017.65 C ATOM 3628 SG CYS B 510 30.852 25.448 18.085 1.00 24.98 S ATOM3629 C CYS B 510 29.772 23.849 14.428 1.00 20.96 C ATOM 3630 O CYS B 51029.602 22.676 14.188 1.00 25.35 O ATOM 3631 N ILE B 511 29.149 24.80313.763 1.00 21.34 N ATOM 3632 CA ILE B 511 28.188 24.473 12.713 1.0026.63 C ATOM 3633 CB ILE B 511 27.286 25.707 12.388 1.00 27.47 C ATOM3634 CG2 ILE B 511 26.264 25.345 11.289 1.00 33.99 C ATOM 3635 CG1 ILE B511 26.574 26.153 13.671 1.00 26.92 C ATOM 3636 CD1 ILE B 511 25.89527.516 13.597 1.00 31.85 C ATOM 3637 C ILE B 511 28.871 23.984 11.4461.00 30.34 C ATOM 3638 O ILE B 511 28.434 22.987 10.848 1.00 29.71 OATOM 3639 N ASN B 512 29.968 24.623 11.058 1.00 25.07 N ATOM 3640 CA ASNB 512 30.615 24.223 9.825 1.00 25.52 C ATOM 3641 CB ASN B 512 31.41625.376 9.236 1.00 23.08 C ATOM 3642 CG ASN B 512 30.539 26.354 8.8171.00 31.89 C ATOM 3643 OD1 ASN B 512 29.466 26.336 8.268 1.00 35.21 OATOM 3644 ND2 ASN B 512 31.000 27.747 9.072 1.00 40.49 N ATOM 3645 C ASNB 512 31.518 23.014 9.970 1.00 30.37 C ATOM 3646 O ASN B 512 31.63322.224 9.045 1.00 30.30 O ATOM 3647 N PHE B 513 32.178 22.874 11.1091.00 23.05 N ATOM 3648 CA PHE B 513 33.084 21.744 11.273 1.00 21.06 CATOM 3649 CB PHE B 513 34.513 22.245 11.303 1.00 21.42 C ATOM 3650 CGPHE B 513 34.924 22.945 10.031 1.00 32.74 C ATOM 3651 CD1 PHE B 51335.063 24.326 10.005 1.00 34.47 C ATOM 3652 CD2 PHE B 513 35.120 22.2168.858 1.00 32.93 C ATOM 3653 CE1 PHE B 513 35.393 24.986 8.805 1.0039.39 C ATOM 3654 CE2 PHE B 513 35.448 22.871 7.664 1.00 40.01 C ATOM3655 CZ PHE B 513 35.581 24.253 7.645 1.00 36.34 C ATOM 3656 C PHE B 51332.856 20.836 12.477 1.00 24.61 C ATOM 3657 O PHE B 513 33.687 19.96812.741 1.00 25.10 O ATOM 3658 N ARG B 514 31.758 21.060 13.207 1.0020.51 N ATOM 3659 CA ARG B 514 31.407 20.266 14.381 1.00 21.86 C ATOM3660 CB ARG B 514 31.062 18.815 13.944 1.00 21.50 C ATOM 3661 CG ARG B514 29.938 17.415 12.935 1.00 22.64 C ATOM 3662 CD ARG B 514 29.43717.550 12.570 1.00 25.89 N ATOM 3663 NE ARG B 514 28.284 17.550 11.6681.00 25.50 N ATOM 3664 CZ ARG B 514 27.531 16.537 11.265 1.00 27.87 CATOM 3665 NH1 ARG B 514 27.803 15.306 11.672 1.00 28.30 N ATOM 3666 NH2ARG B 514 26.476 16.760 10.478 1.00 28.78 N ATOM 3667 C ARG B 514 32.56020.260 15.395 1.00 21.80 C ATOM 3668 O ARG B 514 32.735 19.299 16.1411.00 23.13 O ATOM 3669 N LYS B 515 33.288 21.373 15.438 1.00 23.39 NATOM 3670 CA LYS B 515 34.442 21.512 16.323 1.00 21.15 C ATOM 3671 CBLYS B 515 35.551 22.203 15.532 1.00 22.48 C ATOM 3672 CG LYS B 51536.848 22.399 16.309 1.00 23.37 C ATOM 3673 CD LYS B 515 37.848 23.19516.490 1.00 30.48 C ATOM 3674 CE LYS B 515 38.992 23.662 16.372 1.0037.06 C ATOM 3675 NZ LYS B 515 39.892 34.621 15.659 1.00 43.43 N ATOM3676 C LYS B 515 34.100 22.315 17.597 1.00 22.11 C ATOM 3677 O LYS B 51533.704 23.477 17.503 1.00 20.32 O ATOM 3678 N PHE B 516 34.302 21.71218.773 1.00 22.31 N ATOM 3679 CA PHE B 516 33.987 22.381 20.045 1.0019.14 C ATOM 3680 CB PHE B 516 32.903 21.592 20.788 1.00 20.60 C ATOM3681 CG PHE B 516 31.585 21.555 20.037 1.00 21.15 C ATOM 3682 CD1 PHE B516 31.411 20.683 18.963 1.00 22.16 C ATOM 3683 CD2 PHE B 516 30.55922.439 20.371 1.00 25.22 C ATOM 3684 CE1 PHE B 516 30.223 20.683 18.2291.00 25.00 C ATOM 3685 CE2 PHE B 516 29.374 22.450 19.629 1.00 23.08 CATOM 3686 CZ PHE B 516 29.209 21.565 18.561 1.00 27.70 C ATOM 3687 C PHEB 516 35.214 22.578 20.911 1.00 19.07 C ATOM 3688 O PHE B 516 36.12721.732 20.908 1.00 21.35 O ATOM 3689 N SER B 517 35.206 23.667 21.6841.00 19.27 N ATOM 3690 CA SER B 517 36.366 24.059 22.496 1.00 26.23 CATOM 3691 CB SER B 517 37.385 24.718 21.542 1.00 24.44 C ATOM 3692 OGSER B 517 36.770 25.861 20.910 1.00 22.44 O ATOM 3693 C SER B 517 35.93525.102 23.528 1.00 21.53 C ATOM 3694 O SER B 517 34.792 25.509 23.5231.00 20.37 O ATOM 3695 N SER B 518 36.836 25.554 24.404 1.00 19.72 NATOM 3696 CA SER B 518 36.435 26.590 25.329 1.00 20.34 C ATOM 3697 CBSER B 518 37.555 26.890 26.341 1.00 27.31 C ATOM 3698 OG SER B 51837.592 25.809 27.275 1.00 32.37 O ATOM 3699 C SER B 518 36.039 27.84224.551 1.00 21.23 C ATOM 3700 O SER B 518 35.165 28.589 24.977 1.0023.54 O ATOM 3701 N ARG B 519 36.689 28.055 23.421 1.00 21.32 N ATOM3702 CA ARG B 519 36.347 29.205 22.610 1.00 18.97 C ATOM 3703 CB ARG B519 37.414 29.420 21.545 1.00 21.22 C ATOM 3704 CG ARG B 519 38.58530.196 22.148 1.00 26.38 C ATOM 3705 CD ARG B 519 39.753 30.191 21.2081.00 35.68 C ATOM 3706 NE ARG B 519 40.851 30.943 21.789 1.00 42.06 NATOM 3707 CZ ARG B 519 42.082 30.952 21.288 1.00 46.57 C ATOM 3708 NH1ARG B 519 42.367 30.246 20.195 1.00 43.72 N ATOM 3709 NH2 ARG B 51943.032 31.653 21.892 1.00 49.64 N ATOM 3710 C ARG B 519 34.964 29.12121.987 1.00 19.81 C ATOM 3711 O ARG B 519 34.363 30.171 21.729 1.0021.27 O ATOM 3712 N SER B 520 34.460 27.909 21.718 1.00 18.58 N ATOM3713 CA SER B 520 33.075 27.864 21.213 1.00 21.84 C ATOM 3714 CB SER B520 32.742 26.535 20.503 1.00 20.81 C ATOM 3715 OG SER B 520 32.90825.379 21.297 1.00 22.92 O ATOM 3716 C SER B 520 32.158 28.162 22.4371.00 23.07 C ATOM 3717 O SER B 520 31.091 28.760 22.290 1.00 21.17 OATOM 3718 N ASP B 521 32.597 27.810 23.649 1.00 19.80 N ATOM 3719 CA ASPB 521 31.824 28.119 24.877 1.00 21.41 C ATOM 3720 CB ASP B 521 32.46227.523 26.150 1.00 28.78 C ATOM 3721 CG ASP B 521 32.050 26.058 26.4091.00 22.85 C ATOM 3722 OD1 ASP B 521 31.099 25.558 25.763 1.00 22.20 OATOM 3723 OD2 ASP B 521 32.683 25.426 27.306 1.00 22.04 O ATOM 3724 CASP B 521 31.827 29.656 25.044 1.00 17.40 C ATOM 3725 O ASP B 521 30.82230.257 25.477 1.00 20.22 O ATOM 3726 N VAL B 522 32.944 30.299 24.6731.00 16.61 N ATOM 3727 CA VAL B 522 32.990 31.785 24.758 1.00 15.75 CATOM 3728 CB VAL B 522 34.397 32.326 24.385 1.00 18.63 C ATOM 3729 CG1VAL B 522 34.392 33.849 24.190 1.00 20.55 C ATOM 3730 CG2 VAL B 52235.377 31.957 25.537 1.00 18.25 C ATOM 3731 C VAL B 522 31.927 32.40223.834 1.00 16.27 C ATOM 3732 O VAL B 522 31.243 33.352 24.221 1.0018.90 O ATOM 3733 N TRP B 523 31.783 31.848 22.634 1.00 17.66 N ATOM3734 CA TRP B 523 30.758 32.371 21.708 1.00 16.82 C ATOM 3735 CB TRP B523 30.805 31.584 20.386 1.00 15.58 C ATOM 3736 CG TRP B 523 29.81332.106 19.335 1.00 17.41 C ATOM 3737 CD2 TRP B 523 30.129 32.847 18.1451.00 19.38 C ATOM 3738 CE2 TRP B 523 28.904 33.164 17.516 1.00 20.03 CATOM 3739 CE3 TRP B 523 31.332 33.280 17.546 1.00 18.44 C ATOM 3740 CD1TRP B 523 28.448 31.999 19.375 1.00 22.97 C ATOM 3741 NE1 TRP B 52327.891 32.641 18.280 1.00 18.65 N ATOM 3742 CZ2 TRP B 523 28.839 33.89516.322 1.00 21.60 C ATOM 3743 CZ3 TRP B 523 31.263 34.010 16.359 1.0019.75 C ATOM 3744 CH2 TRP B 523 30.030 34.313 15.728 1.00 19.91 C ATOM3745 C TRP B 523 29.373 32.241 22.358 1.00 18.12 C ATOM 3746 O TRP B 52328.573 33.189 22.321 1.00 19.38 O ATOM 3747 N SER B 524 29.088 31.08222.956 1.00 17.71 N ATOM 3748 CA SER B 524 27.791 30.853 23.643 1.0022.69 C ATOM 3749 CB SER B 524 27.740 29.419 24.213 1.00 21.28 C ATOM3750 OG SER B 524 27.817 28.467 23.185 1.00 31.98 O ATOM 3751 C SER B524 27.579 31.829 24.792 1.00 22.41 C ATOM 3752 O SER B 524 26.46432.331 25.014 1.00 18.61 O ATOM 3753 N TYR B 525 28.644 32.099 25.5461.00 22.85 N ATOM 3754 CA TYR B 525 28.619 33.051 26.640 1.00 21.01 CATOM 3755 CB TYR B 525 30.040 33.201 27.268 1.00 19.16 C ATOM 3756 CGTYR B 525 30.046 34.181 28.409 1.00 20.09 C ATOM 3757 CD1 TYR B 52529.456 33.865 26.638 1.00 21.83 C ATOM 3758 CE1 TYR B 525 29.411 34.80630.692 1.00 20.51 C ATOM 3759 CD2 TYR B 525 30.602 35.461 28.251 1.0019.44 C ATOM 3760 CE2 TYR B 525 30.553 36.400 29.286 1.00 21.12 C ATOM3761 CZ TYR B 525 29.956 36.066 30.501 1.00 26.32 C ATOM 3762 OH TYR B525 29.911 36.999 31.518 1.00 24.81 O ATOM 3763 C TYR B 525 28.15934.407 26.098 1.00 20.91 C ATOM 3764 O TYR B 525 27.344 35.092 26.7181.00 20.39 O ATOM 3765 N GLY B 526 28.711 34.811 24.950 1.00 18.42 NATOM 3766 CA GLY B 526 28.306 36.086 24.357 1.00 19.09 C ATOM 3767 C GLYB 526 26.803 36.116 34.081 1.00 16.71 C ATOM 3768 O GLY B 526 26.13537.118 24.371 1.00 19.95 O ATOM 3769 N VAL B 527 26.271 35.039 23.5061.00 19.63 N ATOM 3770 CA VAL B 527 24.821 34.980 23.240 1.00 17.92 CATOM 3771 CB VAL B 527 24.470 33.705 22.461 1.00 18.12 C ATOM 3772 CG1VAL B 527 22.943 33.645 22.145 1.00 19.94 C ATOM 3773 CG2 VAL B 52725.270 33.697 21.122 1.00 19.40 C ATOM 3774 C VAL B 527 24.082 35.02624.600 1.00 20.57 C ATOM 3775 O VAL B 527 23.063 35.686 24.735 1.0021.39 O ATOM 3776 N THR B 528 24.633 34.377 25.619 1.00 20.54 N ATOM3777 CA THR B 528 24.010 34.397 26.949 1.00 18.80 C ATOM 3778 CB THR B528 24.768 33.458 27.906 1.00 20.59 C ATOM 3779 OG1 THR B 528 24.67332.114 27.395 1.00 21.50 O ATOM 3780 CG2 THR B 528 24.169 33.499 29.2871.00 22.95 C ATOM 3781 C THR B 528 23.981 35.821 27.507 1.00 25.29 CATOM 3782 O THR B 528 22.972 36.235 28.084 1.00 19.03 O ATOM 3783 N METB 529 25.083 36.560 27.337 1.00 21.53 N ATOM 3784 CA MET B 529 25.14737.955 27.789 1.00 20.49 C ATOM 3785 CB MET B 529 26.479 38.621 37.3601.00 20.90 C ATOM 3786 CG MET B 529 27.726 38.072 28.092 1.00 22.65 CATOM 3787 SD MET B 529 29.178 39.101 27.591 1.00 24.81 S ATOM 3788 CEMET B 529 28.792 40.693 28.291 1.00 22.12 C ATOM 3789 C MET B 529 24.01338.740 27.103 1.00 19.53 C ATOM 3790 O MET B 529 23.331 39.551 27.7391.00 20.14 O ATOM 3791 N TRP B 530 23.843 38.505 25.802 1.00 20.92 NATOM 3792 CA TRP B 530 22.800 39.234 25.035 1.00 19.60 C ATOM 3793 CBTRP B 530 22.848 38.845 23.556 1.00 20.03 C ATOM 3794 CG TRP B 53021.996 39.725 22.693 1.00 18.41 C ATOM 3795 CD2 TRP B 530 20.610 39.53322.395 1.00 19.07 C ATOM 3796 CE2 TRP B 530 20.191 40.635 21.590 1.0020.94 C ATOM 3797 CE3 TRP B 530 19.678 38.543 22.726 1.00 22.34 C ATOM3798 CD1 TRP B 530 22.373 40.909 22.072 1.00 18.66 C ATOM 3799 NE1 TRP B530 21.276 41.460 21.399 1.00 21.22 N ATOM 3800 CZ2 TRP B 530 18.86640.762 21.116 1.00 26.05 C ATOM 3801 CZ3 TRP B 530 18.369 38.673 22.2541.00 23.03 C ATOM 3802 CH2 TRP B 530 17.978 39.770 21.462 1.00 27.41 CATOM 3803 C TRP B 530 21.403 38.947 25.567 1.00 21.14 C ATOM 3804 O TRPB 530 20.607 39.880 25.807 1.00 22.19 O ATOM 3805 N GLU B 531 21.10137.665 25.754 1.00 21.34 N ATOM 3806 CA GLU B 531 19.799 37.234 26.2881.00 22.58 C ATOM 3807 CB GLU B 531 19.785 35.725 26.566 1.00 23.47 CATOM 3808 CG GLU B 531 19.941 34.786 25.384 1.00 26.14 C ATOM 3809 CDGLU B 531 19.873 33.318 25.844 1.00 26.77 C ATOM 3810 OE1 GLU B 53120.953 32.715 26.078 1.00 22.88 O ATOM 3811 OE2 GLU B 531 18.731 32.78825.983 1.00 27.11 O ATOM 3812 C GLU B 531 19.548 37.897 27.617 1.0020.02 C ATOM 3813 O GLU B 531 18.432 38.384 27.895 1.00 23.77 O ATOM3814 N ALA B 532 20.565 37.903 28.478 1.00 20.17 N ATOM 3815 CA ALA B532 20.408 38.497 29.795 1.00 18.65 C ATOM 3816 CB ALA B 532 21.61738.155 30.711 1.00 20.90 C ATOM 3817 C ALA B 532 20.204 39.994 29.7761.00 24.11 C ATOM 3818 O ALA B 532 19.290 40.506 30.425 1.00 20.67 OATOM 3819 N LEU B 533 21.062 40.701 29.045 1.00 24.27 N ATOM 3820 CA LEUB 533 20.980 42.163 28.975 1.00 28.04 C ATOM 3821 CB LEU B 533 22.28242.737 28.376 1.00 22.81 C ATOM 3822 CG LEU B 533 23.472 42.615 29.3451.00 21.62 C ATOM 3823 CD1 LEU B 533 24.801 42.869 28.608 1.00 29.89 CATOM 3824 CD2 LEU B 533 23.309 43.620 30.508 1.00 25.39 C ATOM 3825 CLEU B 533 19.745 42.629 28.194 1.00 26.38 C ATOM 3826 O LEU B 533 19.35243.810 28.275 1.00 22.57 O ATOM 3827 N SER B 534 19.122 41.702 27.4641.00 21.44 N ATOM 3828 CA SER B 534 17.888 41.991 26.714 1.00 23.07 CATOM 3829 CB SER B 534 17.862 41.187 25.249 1.00 21.95 C ATOM 3830 OGSER B 534 18.842 41.679 25.534 1.00 31.02 O ATOM 3831 C SER B 534 16.70941.560 27.562 1.00 24.51 C ATOM 3832 O SER B 534 15.571 41.538 27.1061.00 27.12 O ATOM 3833 N TYR B 535 17.000 41.199 28.803 1.00 25.92 NATOM 3834 CA TYR B 535 15.990 40.738 39.739 1.00 28.32 C ATOM 3835 CBTYR B 535 15.102 41.910 30.198 1.00 28.47 C ATOM 3836 CG TYR B 53515.858 42.811 31.144 1.00 29.31 C ATOM 3837 CD1 TYR B 535 16.777 43.733330.652 1.00 28.02 C ATOM 3838 CE1 TYR B 535 17.563 44.492 31.511 1.0029.55 C ATOM 3839 CD2 TYR B 535 15.736 42.679 32.526 1.00 28.97 C ATOM3840 CE2 TYR B 535 16.514 43.434 33.395 1.00 30.17 C ATOM 3841 CZ TYR B535 17.431 44.341 32.874 1.00 22.54 C ATOM 3842 OH TYR B 535 18.18545.117 33.713 1.00 29.23 O ATOM 3843 C TYR B 535 15.137 39.579 29.2241.00 30.50 C ATOM 3844 O TYR B 535 13.918 39.637 29.245 1.00 29.15 OATOM 3845 N GLY B 536 15.805 38.525 28.754 1.00 25.34 N ATOM 3846 CA GLYB 536 15.090 37.334 28.313 1.00 26.66 C ATOM 3847 C GLY B 536 14.56337.236 26.907 1.00 28.90 C ATOM 3848 O GLY B 536 13.831 36.301 26.5831.00 34.84 O ATOM 3849 N GLN B 537 14.940 38.177 26.044 1.00 30.40 NATOM 3850 CA GLN B 537 14.504 38.138 24.658 1.00 28.41 C ATOM 3851 CBGLN B 537 14.840 39.463 23.973 1.00 32.82 C ATOM 3852 CG GLN B 53713.837 40.571 24.309 1.00 43.11 C ATOM 3853 CD GLN B 537 14.217 41.92023.731 1.00 47.65 C ATOM 3854 OE1 GLN B 537 14.599 42.029 22.562 1.0054.72 O ATOM 3855 NE2 GLN B 537 14.108 42.961 24.547 1.00 50.31 N ATOM3856 C GLN B 537 15.175 36.979 23.918 1.00 30.53 C ATOM 3857 O GLN B 53716.238 36.507 24.326 1.00 25.81 O ATOM 3858 N LYS B 538 14.550 36.51522.832 1.00 26.52 N ATOM 3859 CA LYS B 538 15.124 35.249 22.060 1.0026.82 C ATOM 3860 CB LYS B 538 14.036 34.673 21.292 1.00 33.23 C ATOM3861 CG LYS B 538 13.077 33.922 22.201 1.00 43.54 C ATOM 3862 CD LYS B538 12.031 33.160 21.393 1.00 44.85 C ATOM 3863 CE LYS B 538 11.27832.173 22.282 1.00 50.77 C ATOM 3864 NZ LYS B 538 10.275 31.376 21.5061.00 55.00 C ATOM 3865 C LYS B 538 16.142 35.971 21.055 1.00 28.86 CATOM 3866 O LYS B 538 15.915 37.005 20.425 1.00 29.11 O ATOM 3867 N PROB 539 17.289 35.290 20.917 1.00 25.45 N ATOM 3868 CD PRO B 539 17.82634.185 21.727 1.00 22.65 C ATOM 3869 CA PRO B 539 18.285 35.763 19.9521.00 24.40 C ATOM 3870 CB PRO B 539 19.518 34.912 20.276 1.00 28.27 CATOM 3871 CG PRO B 539 18.920 33.647 20.824 1.00 33.25 C ATOM 3872 C PROB 539 17.828 35.548 18.507 1.00 28.17 C ATOM 3873 O PRO B 539 17.13634.584 18.201 1.00 25.84 O ATOM 3874 N TYR B 540 18.229 36.458 17.6301.00 22.91 N ATOM 3875 CA TYR B 540 17.918 36.423 16.206 1.00 26.70 CATOM 3876 CB TYR B 540 18.740 35.333 15.518 1.00 23.59 C ATOM 3877 CGTYR B 540 20.240 35.373 15.839 1.00 29.92 C ATOM 3878 CD1 TYR B 54021.094 36.237 15.163 1.00 24.88 C ATOM 3879 CE1 TYR B 540 22.470 36.26415.447 1.00 24.04 C ATOM 3880 CD2 TYR B 540 20.773 34.542 16.821 1.0028.81 C ATOM 3881 CE2 TYR B 540 22.153 34.568 17.142 1.00 22.99 C ATOM3882 CZ TYR B 540 22.988 35.424 16.443 1.00 20.60 C ATOM 3883 OH TYR B540 24.327 35.447 16.724 1.00 23.56 O ATOM 3884 C TYR B 540 16.43536.134 16.017 1.00 25.23 C ATOM 3885 O TYR B 540 16.063 35.273 15.2241.00 28.39 O ATOM 3886 N LYS B 541 15.637 36.889 16.769 1.00 28.66 NATOM 3887 CA LYS B 541 14.186 36.785 16.823 1.00 40.37 C ATOM 3888 CBLYS B 541 13.642 38.072 17.450 1.00 43.79 C ATOM 3888 CG LYS B 54112.245 37.962 18.030 1.00 55.46 C ATOM 3890 CD LYS B 541 11.876 39.21118.856 1.00 55.84 C ATOM 3891 CE LYS B 541 12.786 39.383 20.081 1.0060.14 C ATOM 3892 NZ LYS B 541 12.345 40.490 20.993 1.00 56.25 N ATOM3893 C LYS B 541 13.502 36.524 15.480 1.00 43.30 C ATOM 3894 O LYS B 54112.731 35.578 15.337 1.00 43.84 O ATOM 3895 N LYS B 542 13.791 37.34914.493 1.00 43.89 N ATOM 3896 CA LYS B 542 13.147 37.178 13.200 1.0050.62 C ATOM 3897 CB LYS B 542 12.893 38.547 12.575 1.00 51.21 C ATOM3898 CG LYS B 542 14.153 39.355 12.339 1.00 56.73 C ATOM 3899 CD LYS B542 13.849 40.636 11.571 1.00 61.48 C ATOM 3900 CE LYS B 542 15.13541.350 11.161 1.00 60.94 C ATOM 3901 NZ LYS B 542 14.892 42.611 10.3951.00 64.23 C ATOM 3902 C LYS B 542 13.921 36.309 12.221 1.00 56.90 CATOM 3903 O LYS B 542 13.821 36.518 11.008 1.00 59.68 O ATOM 3904 N METB 543 14.663 35.322 12.724 1.00 41.97 N ATOM 3905 CA MET B 543 15.44334.453 11.844 1.00 45.64 C ATOM 3906 CB MET B 543 16.952 34.817 11.9071.00 43.71 C ATOM 3907 CG MET B 543 17.348 35.994 11.066 1.00 53.65 CATOM 3908 SD MET B 543 19.100 36.330 11.367 1.00 42.99 S ATOM 3909 CEMET B 543 18.961 37.898 12.209 1.00 45.52 C ATOM 3910 C MET B 543 15.33232.979 12.173 1.00 47.61 C ATOM 3911 O MET B 543 15.075 32.599 13.3181.00 48.77 O ATOM 3912 N LYS B 544 15.562 32.152 11.157 1.00 48.07 NATOM 3913 CA LYS B 544 15.522 30.704 11.301 1.00 54.78 C ATOM 3914 CBLYS B 544 14.693 30.079 10.181 1.00 55.48 C ATOM 3915 CG LYS B 54415.303 30.244 8.792 1.00 64.05 C ATOM 3916 CD LYS B 544 14.493 29.4917.739 1.00 64.50 C ATOM 3917 CE LYS B 544 15.167 29.517 6.367 1.00 65.75C ATOM 3918 NZ LYS B 544 14.420 28.692 5.363 1.00 63.25 N ATOM 3919 CLYS B 544 16.953 30.168 11.231 1.00 56.68 C ATOM 3920 O LYS B 544 17.90830.904 11.473 1.00 54.87 O ATOM 3921 N GLY B 545 17.092 28.890 10.8851.00 54.19 N ATOM 3922 CA GLY B 545 18.408 28.280 10.805 1.00 54.15 CATOM 3923 C GLY B 545 19.352 28.912 9.797 1.00 50.65 C ATOM 3924 O GLY B545 20.219 29.694 10.174 1.00 52.75 O ATOM 3925 N PRO B 546 19.21328.585 8.504 1.00 50.84 N ATOM 3926 CD PRO B 546 18.223 27.634 7.9651.00 54.61 C ATOM 3927 CA PRO B 546 20.056 29.110 7.423 1.00 51.43 CATOM 3928 CB PRO B 546 19.341 28.613 6.164 1.00 52.58 C ATOM 3929 CG PROB 546 18.809 27.294 6.609 1.00 51.61 C ATOM 3930 C PRO B 546 20.24130.624 7.416 1.00 45.67 C ATOM 3931 O PRO B 546 21.274 31.128 6.963 1.0040.66 O ATOM 3932 N GLU B 547 19.234 31.343 7.903 1.00 40.50 N ATOM 3933CA GLU B 547 19.294 32.796 7.953 1.00 44.42 C ATOM 3934 CB GLU B 54717.963 33.376 8.410 1.00 44.41 C ATOM 3935 CG GLU B 547 16.811 33.0937.475 1.00 59.26 C ATOM 3936 CD GLU B 547 15.538 33.763 7.927 1.00 56.22C ATOM 3937 OE1 GLU B 547 15.479 35.013 7.898 1.00 62.09 O ATOM 3938 OE2GLU B 547 14.603 33.037 8.319 1.00 59.62 O ATOM 3939 C GLU B 547 20.39133.282 8.902 1.00 35.91 C ATOM 3940 O GLU B 547 21.149 34.172 8.555 1.0034.83 O ATOM 3941 N VAL B 548 20.460 32.694 10.094 1.00 36.33 N ATOM3942 CA VAL B 548 21.473 33.108 11.080 1.00 26.71 C ATOM 3943 CB VAL B548 21.252 32.396 12.420 1.00 35.48 C ATOM 3944 CG1 VAL B 548 22.28532.872 13.448 1.00 32.82 C ATOM 3945 CG2 VAL B 548 19.847 32.688 12.9171.00 40.22 C ATOM 3946 C VAL B 548 22.890 32.843 10.591 1.00 31.26 CATOM 3947 O VAL B 548 23.762 33.696 10.708 1.00 33.92 O ATOM 3948 N METB 549 23.125 31.663 10.027 1.00 31.21 N ATOM 3949 CA MET B 549 24.43931.316 9.511 1.00 35.46 C ATOM 3950 CB MET B 549 24.397 29.909 8.9081.00 40.89 C ATOM 3951 CG MET B 549 25.766 29.271 8.799 1.00 51.71 CATOM 3952 SD MET B 549 26.636 29.238 10.404 1.00 72.82 S ATOM 3953 CEMET B 549 27.806 30.616 10.266 1.00 56.71 C ATOM 3954 C MET B 549 24.91832.325 8.445 1.00 31.51 C ATOM 3955 O MET B 549 26.050 32.788 8.479 1.0031.13 O ATOM 3956 N ALA B 550 24.042 32.645 7.501 1.00 32.16 N ATOM 3957CA ALA B 550 24.373 33.588 6.431 1.00 33.32 C ATOM 3958 CB ALA B 55023.206 33.653 5.428 1.00 37.58 C ATOM 3959 C ALA B 550 24.656 34.9797.014 1.00 25.47 C ATOM 3960 O ALA B 550 25.568 35.680 6.578 1.00 29.24O ATOM 3961 N PHE B 551 23.857 35.360 8.007 1.00 25.23 N ATOM 3962 CAPHE B 551 23.975 36.647 8.706 1.00 28.55 C ATOM 3963 CB PHE B 551 22.85236.714 9.769 1.00 20.31 C ATOM 3964 CG PHE B 551 22.783 38.000 10.5431.00 29.64 C ATOM 3965 CD1 PHE B 551 22.226 39.144 9.973 1.00 28.55 CATOM 3966 CD2 PHE B 551 23.209 38.052 11.876 1.00 29.88 C ATOM 3967 CE1PHE B 551 22.081 40.319 10.716 1.00 26.70 C ATOM 3968 CE2 PHE B 55123.066 39.232 12.636 1.00 26.29 C ATOM 3969 CZ PHE B 551 22.498 40.36212.050 1.00 31.05 C ATOM 3970 C PHE B 551 25.354 36.743 9.361 1.00 26.40C ATOM 3971 O PHE B 551 26.084 37.721 9.188 1.00 22.68 O ATOM 3972 N ILEB 552 25.717 35.720 10.123 1.00 23.43 N ATOM 3973 CA ILE B 552 27.02235.707 10.778 1.00 21.41 C ATOM 3974 CB ILE B 552 27.135 34.460 11.6811.00 26.93 C ATOM 3975 CG2 ILE B 552 28.553 34.320 12.206 1.00 28.00 CATOM 3976 CG1 ILE B 552 26.046 34.533 12.764 1.00 27.40 C ATOM 3977 CD1ILE B 552 26.179 35.709 13.768 1.00 29.73 C ATOM 3978 C ILE B 552 28.14635.706 9.737 1.00 22.04 C ATOM 3979 O ILE B 552 29.139 36.428 9.871 1.0025.44 O ATOM 3980 N GLU B 553 27.988 34.910 8.684 1.00 25.85 N ATOM 3981CA GLU B 553 29.004 34.842 7.630 1.00 30.95 C ATOM 3982 CB GLU B 55328.613 33.796 6.580 1.00 40.19 C ATOM 3983 CG GLU B 553 28.654 32.3607.092 1.00 48.42 C ATOM 3984 CD GLU B 553 30.068 31.858 7.339 1.00 49.16C ATOM 3985 OE1 GLU B 553 30.212 30.786 7.970 1.00 54.92 O ATOM 3986 OE2GLU B 553 31.030 32.525 6.896 1.00 56.67 O ATOM 3987 C GLU B 553 29.22036.206 6.947 1.00 29.01 C ATOM 3988 O GLU B 553 30.331 36.527 6.525 1.0034.32 O ATOM 3989 N GLN B 554 28.152 36.988 6.835 1.00 30.24 N ATOM 3990CA GLN B 554 28.214 38.324 6.240 1.00 33.67 C ATOM 3991 CB GLN B 55426.806 38.870 6.010 1.00 35.02 C ATOM 3992 CG GLN B 554 26.026 38.2244.891 1.00 47.06 C ATOM 3993 CD GLN B 554 24.620 38.761 4.858 1.00 45.80C ATOM 3994 OE1 GLN B 554 24.410 39.970 5.004 1.00 52.95 O ATOM 3995 NE2GLN B 554 23.647 37.874 4.669 1.00 52.85 N ATOM 3996 C GLN B 554 28.94039.308 7.154 1.00 35.79 C ATOM 3997 O GLN B 554 29.176 40.452 6.772 1.0029.12 O ATOM 3998 N GLY B 555 29.274 38.871 8.366 1.00 26.81 N ATOM 3999CA GLY B 555 29.960 39.765 9.284 1.00 29.43 C ATOM 4000 C GLY B 55529.025 40.644 10.119 1.00 27.00 C ATOM 4001 O GLY B 555 29.447 41.67210.660 1.00 26.99 O ATOM 4002 N LYS B 556 27.759 40.257 10.231 1.0020.65 N ATOM 4003 CA LYS B 556 26.826 41.024 11.045 1.00 21.47 C ATOM4004 CB LYS B 556 25.489 41.198 10.315 1.00 24.59 C ATOM 4005 CG LYS B556 25.631 41.916 8.959 1.00 24.98 C ATOM 4006 CD LYS B 556 24.28042.165 8.338 1.00 24.97 C ATOM 4007 CE LYS B 556 24.429 42.911 6.9901.00 31.95 C ATOM 4008 NZ LYS B 556 23.084 43.238 6.391 1.00 32.23 NATOM 4009 C LYS B 556 26.580 40.283 12.364 1.00 22.25 C ATOM 4010 O LYSB 556 26.701 39.057 12.431 1.00 21.17 O ATOM 4011 N ARG B 557 26.20841.049 13.384 1.00 20.82 N ATOM 4012 CA ARG B 557 25.950 40.496 14.7091.00 22.17 C ATOM 4013 CB ARG B 557 27.164 40.778 15.629 1.00 19.79 CATOM 4014 CG ARG B 557 28.487 40.159 15.124 1.00 21.41 C ATOM 4015 CDARG B 557 28.495 38.618 15.195 1.00 19.59 C ATOM 4016 NE ARG B 55729.796 38.029 14.814 1.00 20.25 N ATOM 4017 CZ ARG B 557 30.161 37.68113.579 1.00 23.23 C ATOM 4018 NH1 ARG B 557 29.329 37.849 12.534 1.0021.34 N ATOM 4019 NH2 ARG B 557 31.354 37.117 13.379 1.00 18.85 N ATOM4020 C ARG B 557 24.699 41.113 15.311 1.00 25.58 C ATOM 4021 O ARG B 55724.163 42.122 14.787 1.00 20.60 O ATOM 4022 N MET B 558 24.211 40.52016.405 1.00 23.12 N ATOM 4023 CA MET B 558 23.031 41.057 17.061 1.0023.08 C ATOM 4024 CB MET B 558 22.577 40.150 18.226 1.00 21.21 C ATOM4025 CG MET B 558 21.929 38.861 17.759 1.00 23.06 C ATOM 4026 SD MET B558 21.172 37.972 19.155 1.00 25.40 S ATOM 4027 CE MET B 558 22.58937.274 19.959 1.00 20.17 C ATOM 4028 C MET B 558 23.299 42.458 17.5881.00 26.20 C ATOM 4029 O MET B 558 24.416 42.787 18.026 1.00 22.21 OATOM 4030 N GLU B 559 22.262 43.287 17.554 1.00 22.33 N ATOM 4031 CA GLUB 559 22.354 44.649 18.023 1.00 25.04 C ATOM 4032 CB GLU B 559 21.04745.392 17.711 1.00 33.85 C ATOM 4033 CG GLU B 559 19.765 44.572 17.9531.00 44.82 C ATOM 4034 CD GLU B 559 19.514 43.500 16.868 1.00 56.27 CATOM 4035 OE1 GLU B 559 19.120 43.868 15.733 1.00 60.02 O ATOM 4036 OE2GLU B 559 19.710 42.290 17.149 1.00 44.19 O ATOM 4037 C GLU B 559 22.64644.778 19.513 1.00 25.59 C ATOM 4038 O GLU B 559 22.362 43.880 20.3021.00 29.33 O ATOM 4039 N CYS B 560 23.210 45.913 19.897 1.00 22.19 NATOM 4040 CA CYS B 560 23.471 46.170 21.306 1.00 25.34 C ATOM 4041 CBCYS B 560 24.313 47.440 21.454 1.00 26.43 C ATOM 4042 SG CYS B 56024.611 47.893 23.164 1.00 30.43 S ATOM 4043 C CYS B 560 22.108 46.33622.013 1.00 32.06 C ATOM 4044 O CYS B 560 21.262 47.124 21.570 1.0029.35 O ATOM 4045 N PRO B 561 21.855 45.564 23.092 1.00 30.63 N ATOM4046 CD PRO B 561 22.644 44.426 23.611 1.00 28.65 C ATOM 4047 CA PRO B561 20.570 45.686 23.803 1.00 31.69 C ATOM 4048 CB PRO B 561 20.72744.723 24.987 1.00 28.11 C ATOM 4049 CG PRO B 561 21.605 43.638 24.4181.00 25.66 C ATOM 4050 C PRO B 561 20.348 47.111 24.298 1.00 28.57 CATOM 4051 O PRO B 561 21.292 47.850 24.542 1.00 26.62 O ATOM 4052 N PROB 562 19.092 47.519 24.459 1.00 37.07 N ATOM 4053 CD PRO B 562 17.85246.840 24.046 1.00 39.32 C ATOM 4054 CA PRO B 562 18.821 48.880 24.9391.00 38.49 C ATOM 4055 CB PRO B 562 17.294 48.942 24.948 1.00 42.66 CATOM 4056 CG PRO B 562 16.920 48.002 23.833 1.00 48.28 C ATOM 4057 C PROB 562 19.419 49.086 26.336 1.00 38.16 C ATOM 4058 O PRO B 562 19.32948.207 27.193 1.00 38.50 O ATOM 4059 N GLU B 563 20.042 50.236 26.5681.00 37.38 N ATOM 4060 CA GLU B 563 20.623 50.530 27.881 1.00 43.37 CATOM 4061 CB GLU B 563 19.564 50.341 28.981 1.00 49.78 C ATOM 4062 CGGLU B 563 18.309 51.190 28.805 1.00 53.84 C ATOM 4063 CD GLU B 56317.088 50.587 29.496 1.00 61.69 C ATOM 4064 OE1 GLU B 563 17.133 50.38930.734 1.00 64.80 O ATOM 4065 OE2 GLU B 563 16.085 50.307 27.795 1.0062.44 O ATOM 4066 C GLU B 563 21.873 49.714 28.228 1.00 42.92 C ATOM4067 O GLU B 563 22.433 49.860 29.314 1.00 46.04 O ATOM 4068 N CYS B 56422.312 48.832 27.332 1.00 40.16 N ATOM 4069 CA CYS B 564 23.527 48.07027.589 1.00 35.91 C ATOM 4070 CB CYS B 564 23.614 46.843 26.662 1.0035.94 C ATOM 4071 SG CYS B 564 25.157 45.907 26.802 1.00 37.39 S ATOM4072 C CYS B 564 24.706 49.006 27.324 1.00 37.21 C ATOM 4073 O CYS B 56424.832 49.559 26.231 1.00 36.78 O ATOM 4074 N PRO B 565 25.580 49.20028.324 1.00 35.01 N ATOM 4075 CD PRO B 565 25.531 48.573 29.655 1.0039.96 C ATOM 4076 CA PRO B 565 26.753 50.072 28.200 1.00 32.47 C ATOM4077 CB PRO B 565 27.382 50.015 29.589 1.00 40.02 C ATOM 4078 CG PRO B565 26.960 48.666 30.098 1.00 43.81 C ATOM 4079 C PRO B 565 27.70949.607 27.127 1.00 35.02 C ATOM 4080 O PRO B 565 27.860 48.403 26.8931.00 34.15 O ATOM 4081 N PRO B 566 28.396 50.558 26.475 1.00 33.68 NATOM 4082 CD PRO B 566 28.297 52.010 26.727 1.00 34.27 C ATOM 4083 CAPRO B 566 29.360 50.272 25.408 1.00 30.53 C ATOM 4084 CB PRO B 56629.908 51.647 25.137 1.00 31.64 C ATOM 4085 CG PRO B 566 28.908 52.60725.481 1.00 31.51 C ATOM 4086 C PRO B 566 30.412 49.223 25.792 1.0031.72 C ATOM 4087 O PRO B 566 30.757 48.379 24.978 1.00 28.48 O ATOM4088 N GLU B 567 30.920 49.285 27.028 1.00 27.33 N ATOM 4089 CA GLU B567 31.960 48.345 27.472 1.00 33.27 C ATOM 4090 CB GLU B 567 32.45148.701 28.894 1.00 36.30 C ATOM 4091 CG GLU B 567 32.553 50.189 29.1921.00 49.34 C ATOM 4092 CD GLU B 567 31.195 50.835 29.391 1.00 50.90 CATOM 4093 OE1 GLU B 567 30.471 50.431 30.330 1.00 63.92 O ATOM 4094 OE2GLU B 567 30.851 51.744 28.612 1.00 47.96 O ATOM 4095 C GLU B 567 31.44046.908 27.485 1.00 26.60 C ATOM 4096 O GLU B 567 32.143 45.964 27.0891.00 25.31 O ATOM 4097 N LEU B 568 30.208 46.747 27.948 1.00 25.52 NATOM 4098 CA LEU B 568 29.590 45.442 28.017 1.00 28.35 C ATOM 4099 CBLEU B 568 28.312 45.549 28.851 1.00 31.11 C ATOM 4100 CG LEU B 56827.993 44.399 29.788 1.00 31.00 C ATOM 4101 CD1 LEU B 568 29.277 43.79630.349 1.00 35.96 C ATOM 4102 CD2 LEU B 568 27.101 44.939 30.912 1.0025.70 C ATOM 4103 C LEU B 568 29.289 44.939 30.912 1.00 25.70 C ATOM4104 O LEU B 568 29.498 43.738 26.341 1.00 22.86 O ATOM 4105 N TYR B 56928.793 45.791 25.733 1.00 23.22 N ATOM 4106 CA TYR B 569 28.538 45.31024.383 1.00 22.95 C ATOM 4107 CB TYR B 569 27.765 46.361 23.542 1.0021.93 C ATOM 4108 CG TYR B 569 27.412 45.828 22.170 1.00 21.83 C ATOM4109 CD1 TYR B 569 26.583 44.721 22.022 1.00 21.17 C ATOM 4110 CE1 TYR B569 26.304 44.169 20.757 1.00 22.67 C ATOM 4111 CD2 TYR B 569 27.96646.396 21.006 1.00 28.53 C ATOM 4112 CE2 TYR B 569 27.703 45.853 19.7391.00 27.28 C ATOM 4113 CZ TYR B 569 26.881 44.746 19.622 1.00 28.33 CATOM 4114 OH TYR B 569 26.664 44.202 18.384 1.00 25.54 O ATOM 4115 C TYRB 569 29.856 44.948 23.683 1.00 19.58 C ATOM 4116 O TYR B 569 29.90943.976 22.908 1.00 23.18 O ATOM 4117 N ALA B 570 30.927 45.704 23.9431.00 23.62 N ATOM 4118 CA ALA B 570 32.206 45.415 23.296 1.00 24.27 CATOM 4119 CB ALA B 570 32.287 46.413 23.739 1.00 26.06 C ATOM 4120 C ALAB 570 32.670 43.993 23.615 1.00 24.88 C ATOM 4121 O ALA B 570 33.22643.307 22.768 1.00 23.64 O ATOM 4122 N LEU B 571 32.443 43.587 24.8561.00 23.04 N ATOM 4123 CA LEU B 571 32.844 42.259 25.336 1.00 21.51 CATOM 4124 CB LEU B 571 32.668 42.201 26.866 1.00 23.34 C ATOM 4125 CGLEU B 571 32.296 40.815 27.465 1.00 22.60 C ATOM 4126 CD1 LEU B 57134.295 40.301 27.028 1.00 24.30 C ATOM 4127 CD2 LEU B 571 32.820 40.91428.981 1.00 24.39 C ATOM 4128 C LEU B 571 31.988 41.197 24.676 1.0016.75 C ATOM 4129 O LEU B 571 32.472 40.189 24.163 1.00 20.66 O ATOM4130 N MET B 572 30.687 41.4277 24.715 1.00 20.93 N ATOM 4131 CA MET B572 29.728 40.535 24.102 1.00 20.96 C ATOM 4132 CB MET B 572 28.35641.204 24.223 1.00 28.64 C ATOM 4133 CG MET B 572 27.271 40.510 23.5021.00 30.16 C ATOM 4134 SD MET B 572 25.729 41.414 23.691 1.00 24.19 SATOM 4135 CE MET B 572 25.754 41.989 25.454 1.00 22.91 C ATOM 4136 C METB 572 30.117 40.358 22.625 1.00 20.33 C ATOM 4137 O MET B 572 30.20439.235 22.101 1.00 20.73 O ATOM 4138 N SER B 573 30.373 41.470 21.9411.00 18.391 N ATOM 4139 CA SER B 573 30.735 41.412 20.528 1.00 21.31 CATOM 4140 CB SER B 573 30.747 42.839 19.939 1.00 25.35 C ATOM 4141 OGSER B 573 31.143 42.855 18.581 1.00 27.38 O ATOM 4142 C SER B 573 32.07340.693 20.296 1.00 23.59 C ATOM 4143 O SER B 573 32.231 39.962 19.3241.00 21.82 O ATOM 4144 N ASP B 574 33.043 40.889 21.176 1.00 22.93 NATOM 4145 CA ASP B 574 34.322 40.196 21.019 1.00 21.19 C ATOM 4146 CBASP B 574 35.363 40.684 22.039 1.00 21.91 C ATOM 4147 CG ASP B 57435.914 42.071 21.707 1.00 25.96 C ATOM 4148 OD1 ASP B 574 35.752 42.55320.567 1.00 23.74 O ATOM 4149 OD2 ASP B 574 36.547 42.667 22.604 1.0026.12 O ATOM 4150 C ASP B 574 34.156 38.667 21.166 1.00 22.88 C ATOM4151 O ASP B 574 34.942 37.915 20.585 1.00 23.63 O ATOM 4152 N CYS B 57533.161 38.218 21.938 1.00 19.59 N ATOM 4153 CA CYS B 575 32.906 36.77822.097 1.00 20.12 C ATOM 4154 CB CYS B 575 31.822 36.522 23.163 1.0022.35 C ATOM 4155 SG CYS B 575 32.353 36.912 24.873 1.00 23.15 S ATOM4156 C CYS B 575 32.426 36.205 20.772 1.00 22.05 C ATOM 4157 O CYS B 57532.442 34.991 20.572 1.00 19.70 O ATOM 4158 N TRP B 576 32.001 37.09619.877 1.00 20.34 N ATOM 4159 CA TRP B 576 31.514 36.699 18.556 1.0019.05 C ATOM 4160 CB TRP B 576 30.184 37.393 18.208 1.00 19.93 C ATOM4161 CG TRP B 576 29.089 37.172 19.205 1.00 22.10 C ATOM 4162 CD2 TRP B576 28.077 38.106 19.558 1.00 17.49 C ATOM 4163 CE2 TRP B 576 27.26327.485 20.547 1.00 18.66 C ATOM 4164 CE3 TRP B 576 27.763 39.414 19.1271.00 16.82 C ATOM 4165 CD1 TRP B 576 28.868 36.045 19.956 1.00 20.31 CATOM 4166 NE1 TRP B 576 27.764 36.225 20.770 1.00 19.04 N ATOM 4167 CZ2TRP B 576 26.158 38.130 21.122 1.00 19.31 C ATOM 4168 CZ3 TRP B 57626.653 40.059 19.692 1.00 19.50 C ATOM 4169 CH2 TRP B 576 25.861 39.41820.684 1.00 19.35 C ATOM 4170 C TRP B 576 32.493 36.958 17.405 1.0022.30 C ATOM 4171 O TRP B 576 32.062 37.191 16.262 1.00 20.73 O ATOM4172 N ILE B 577 33.792 36.942 17.714 1.00 19.99 N ATOM 4173 CA ILE B577 34.826 37.103 16.689 1.00 21.32 C ATOM 4174 CB ILE B 577 36.21537.309 17.338 1.00 20.92 C ATOM 4175 CG2 ILE B 577 37.351 36.977 16.3231.00 19.24 C ATOM 4176 CG1 ILE B 577 36.318 38.764 17.847 1.00 26.98 CATOM 4177 CD1 ILE B 577 37.577 39.046 18.674 1.00 31.70 C ATOM 4178 CILE B 577 34.774 35.798 15.891 1.00 22.46 C ATOM 4179 O ILE B 577 34.78934.707 16.468 1.00 22.10 O ATOM 4180 N TYR B 578 34.673 35.914 14.5711.00 20.33 N ATOM 4181 CA TYR B 578 34.532 34.751 13.715 1.00 24.28 CATOM 4182 CB TYR B 578 34.387 35.200 12.248 1.00 24.92 C ATOM 4183 CGTYR B 578 33.925 34.103 11.307 1.00 25.66 C ATOM 4184 CD1 TYR B 57832.574 33.963 10.977 1.00 29.87 C ATOM 4185 CE1 TYR B 578 32.139 32.91810.134 1.00 32.04 C ATOM 4186 CD2 TYR B 578 34.831 33.173 10.770 1.0031.85 C ATOM 4187 CE2 TYR B 578 34.397 32.126 9.938 1.00 29.55 C ATOM4188 CZ TYR B 578 33.047 32.009 9.628 1.00 31.34 C ATOM 4189 OH TYR B578 32.596 30.972 8.824 1.00 31.73 O ATOM 4190 C TYR B 578 35.648 33.71513.814 1.00 29.60 C ATOM 4191 O TYR B 578 35.377 32.529 14.014 1.0021.86 O ATOM 4192 N LYS B 579 36.887 34.175 13.614 1.00 24.49 N ATOM4193 CA LYS B 579 38.069 33.335 13.631 1.00 27.75 C ATOM 4194 CB LYS B579 39.301 34.121 13.145 1.00 30.85 C ATOM 4195 CG LYS B 579 39.21234.623 11.695 1.00 39.76 C ATOM 4196 CD LYS B 579 40.550 35.234 11.2131.00 43.80 C ATOM 4197 CE LYS B 579 40.481 35.643 9.735 1.00 52.66 CATOM 4198 NZ LYS B 579 41.684 36.457 9.382 1.00 53.08 N ATOM 4199 C LYSB 579 38.346 32.811 15.021 1.00 28.50 C ATOM 4200 O LYS B 579 38.58533.568 15.942 1.00 27.27 O ATOM 4201 N TRP B 580 38.335 31.495 15.1281.00 27.56 N ATOM 4202 CA TRP B 580 38.574 30.806 16.385 1.00 33.99 CATOM 4203 CB TRP B 580 38.649 29.310 16.079 1.00 33.38 C ATOM 4204 CGTRP B 580 38.850 28.472 17.259 1.00 38.62 C ATOM 4205 CD2 TRP B 58040.063 27.818 17.639 1.00 38.34 C ATOM 4206 CE2 TRP B 580 39.793 27.09718.830 1.00 42.10 C ATOM 4207 CE3 TRP B 580 41.354 27.768 17.091 1.0043.21 C ATOM 4208 CD1 TRP B 580 37.920 28.145 18.199 1.00 40.63 C ATOM4209 NE1 TRP B 580 38.479 27.312 19.150 1.00 37.48 N ATOM 4210 CZ2 TRP B580 40.767 26.33 19.484 1.00 42.20 C ATOM 4211 CZ3 TRP B 580 42.32827.004 17.742 1.00 44.42 C ATOM 4212 CH2 TRP B 580 42.025 26.297 18.9271.00 49.85 C ATOM 4213 C TRP B 580 39.862 31.267 17.077 1.00 29.68 CATOM 4214 O TRP B 580 39.862 31.591 18.262 1.00 30.01 O ATOM 4215 N GLUB 581 40.962 31.306 16.336 1.00 27.48 N ATOM 4216 CA GLU B 581 42.23631.710 16.917 1.00 27.95 C ATOM 4217 CB GLU B 581 43.349 31.535 15.8751.00 41.30 C ATOM 4218 CG GLU B 581 43.080 30.409 14.878 1.00 45.98 CATOM 4219 CD GLU B 581 42.292 20.894 13.672 1.00 53.35 C ATOM 4220 OE1GLU B 581 42.833 31.742 12.919 1.00 61.50 O ATOM 4221 OE2 GLU B 58141.144 30.422 13.466 1.00 44.26 O ATOM 4222 C GLU B 581 42.269 33.14117.458 1.00 31.33 C ATOM 4223 O GLU B 581 43.070 33.449 18.327 1.0033.50 O ATOM 4224 N ASP B 582 41.386 34.006 16.961 1.00 28.16 N ATOM4225 CA ASP B 582 41.341 35.407 17.389 1.00 24.75 C ATOM 4226 CB ASP B582 41.073 36.298 16.169 1.00 29.45 C ATOM 4227 CG ASP B 582 42.17936.201 15.131 1.00 39.01 C ATOM 4228 OD1 ASP B 582 43.301 35.821 15.5241.00 35.67 O ATOM 4229 OD2 ASP B 582 41.937 36.495 13.937 1.00 38.00 OATOM 4230 C ASP B 582 40.307 35.726 18.478 1.00 26.77 C ATOM 4231 O ASPB 582 40.250 36.848 18.993 1.00 25.92 O ATOM 4232 N ARG B 583 39.48734.744 18.816 1.00 27.16 N ATOM 4233 CA ARG B 583 38.448 34.959 19.8181.00 29.93 C ATOM 4234 CB ARG B 583 37.324 33.921 19.611 1.00 23.20 CATOM 4235 CG ARG B 583 35.974 34.196 20.334 1.00 20.53 C ATOM 4236 CDARG B 583 34.993 33.051 20.050 1.00 17.55 C ATOM 4237 NE ARG B 58334.872 32.798 18.608 1.00 17.49 N ATOM 4238 CZ ARG B 583 34.658 31.61018.055 1.00 22.33 C ATOM 4239 NH1 ARG B 583 34.528 30.522 18.811 1.0020.02 N ATOM 4240 NH2 ARG B 583 34.618 31.501 16.721 1.00 21.31 N ATOM4241 C ARG B 583 39.101 34.827 21.203 1.00 26.43 C ATOM 4242 O ARG B 58339.964 33.975 21.417 1.00 24.85 O ATOM 4243 N PRO B 584 38.694 35.67922.159 1.00 23.83 N ATOM 4244 CD PRO B 584 37.731 36.791 22.028 1.0023.73 C ATOM 4245 CA PRO B 584 39.252 35.638 23.516 1.00 25.03 C ATOM4246 CB PRO B 584 38.660 36.877 24.178 1.00 25.59 C ATOM 4247 CG PRO B584 37.346 37.053 23.469 1.00 24.23 C ATOM 4248 C PRO B 584 38.89034.383 24.302 1.00 25.66 C ATOM 4249 O PRO B 584 37.896 33.722 23.9871.00 22.86 O ATOM 4250 N ASP B 585 39.714 34.082 25.314 1.00 20.92 NATOM 4251 CA ASP B 585 39.492 32.946 26.205 1.00 23.08 C ATOM 4252 CBASP B 585 40.833 32.346 26.685 1.00 32.60 C ATOM 4253 CG ASP B 58541.670 31.806 25.541 1.00 38.55 C ATOM 4254 OD1 ASP B 585 41.153 31.01224.727 1.00 48.57 O ATOM 4255 OD2 ASP B 585 42.865 32.180 25.469 1.0055.39 O ATOM 4256 C ASP B 585 38.763 33.456 27.448 1.00 20.51 C ATOM4257 O ASP B 585 38.686 34.667 27.668 1.00 23.27 O ATOM 4258 N PHE B 58638.260 32.542 28.286 1.00 21.45 N ATOM 4259 CA PHE B 586 37.538 32.96729.485 1.00 26.29 C ATOM 4260 CB PHE B 586 36.795 31.794 30.151 1.0022.81 C ATOM 4261 CG PHE B 586 35.482 31.470 29.484 1.00 22.63 C ATOM4262 CD1 PHE B 586 34.406 32.367 29.542 1.00 24.53 C ATOM 4263 CD2 PHE B586 35.323 30.268 27.785 1.00 26.40 C ATOM 4264 CE1 PHE B 586 33.17932.049 28.910 1.00 18.28 C ATOM 4265 CE2 PHE B 586 34.112 29.961 28.1611.00 24.68 C ATOM 4266 CZ PHE B 586 33.048 30.847 28.231 1.00 19.51 CATOM 4267 C PHE B 586 38.440 33.673 30.486 1.00 24.38 C ATOM 4268 O PHEB 586 37.983 34.473 31.267 1.00 23.72 O ATOM 4269 N LEU B 587 39.74133.395 30.440 1.00 27.00 N ATOM 4270 CA LEU B 587 40.650 34.114 31.3371.00 24.91 C ATOM 4271 CB LEU B 587 42.093 33.688 31.039 1.00 32.67 CATOM 4272 CG LEU B 587 43.216 34.188 31.943 1.00 43.71 C ATOM 4273 CD1LEU B 587 43.348 35.672 31.784 1.00 43.71 C ATOM 4274 CD2 LEU B 58743.926 33.834 33.380 1.00 40.03 C ATOM 4275 C LEU B 587 40.455 35.62731.103 1.00 23.16 C ATOM 4276 O LEU B 587 40.225 36.374 32.063 1.0026.74 O ATOM 4277 N THR B 588 40.494 36.088 29.852 1.00 23.64 N ATOM4278 CA THR B 588 40.294 37.516 29.607 1.00 22.82 C ATOM 4279 CB THR B588 40.852 37.982 28.299 1.00 33.41 C ATOM 4280 OG1 THR B 588 40.04337.479 27.172 1.00 46.39 O ATOM 4281 CG2 THR B 588 42.266 37.477 28.0561.00 31.62 C ATOM 4282 C THR B 588 38.832 37.929 29.711 1.00 22.83 CATOM 4283 O THR B 588 38.539 39.006 30.205 1.00 27.35 O ATOM 4284 N VALB 589 37.915 37.069 29.258 1.00 23.23 N ATOM 4285 CA VAL B 589 36.50237.418 29.370 1.00 23.31 C ATOM 4286 CB VAL B 589 35.601 36.298 28.7591.00 25.23 C ATOM 4287 CG1 VAL B 589 34.128 36.521 29.142 1.00 24.91 CATOM 4288 CG2 VAL B 589 35.751 36.315 27.238 1.00 24.02 C ATOM 4289 CVAL B 589 36.082 37.688 30.816 1.00 21.77 C ATOM 4290 O VAL B 589 35.38438.666 31.097 1.00 21.67 O ATOM 4291 N GLU B 590 36.503 36.817 31.7361.00 24.09 N ATOM 4292 CA GLU B 590 36.158 36.986 33.149 1.00 23.44 CATOM 4293 CB GLU B 590 36.700 35.792 33.980 1.00 23.66 C ATOM 4294 CGGLU B 590 36.346 35.806 35.489 1.00 28.31 C ATOM 4295 CD GLU B 59037.173 36.793 36.342 1.00 30.31 C ATOM 4296 OE1 GLU B 590 38.375 36.99036.060 1.00 30.33 O ATOM 4297 OE2 GLU B 590 36.623 37.345 37.325 1.0030.51 O ATOM 4298 C GLU B 590 36.722 38.300 33.698 1.00 24.63 C ATOM4299 O GLU B 590 36.060 38.995 34.469 1.00 21.17 O ATOM 4300 N GLN B 59137.948 38.645 33.304 1.00 23.83 N ATOM 4301 CA GLN B 591 38.550 39.89633.775 1.00 25.38 C ATOM 4302 CB GLN B 591 40.005 39.980 33.324 1.0027.76 C ATOM 4303 CG GLN B 591 40.877 38.896 33.902 1.00 36.74 C ATOM4304 CD GLN B 591 42.333 39.101 33.554 1.00 43.26 C ATOM 4305 OE1 GLN B591 42.669 39.908 32.677 1.00 44.86 O ATOM 4306 NE2 GLN B 591 43.20638.370 34.230 1.00 44.68 N ATOM 4307 C GLN B 591 37.818 41.132 33.2791.00 25.08 C ATOM 4308 O GLN B 591 37.616 42.102 34.019 1.00 26.57 OATOM 4309 N ARG B 592 37.423 41.110 32.012 1.00 23.67 N ATOM 4310 CA ARGB 592 36.712 42.239 31.437 1.00 25.81 C ATOM 4311 CB ARG B 592 36.63142.087 29.917 1.00 23.30 C ATOM 4312 CG ARG B 592 38.018 42.247 29.2761.00 31.02 C ATOM 4313 CD ARG B 592 38.006 41.980 27.792 1.00 31.50 CATOM 4314 NE ARG B 592 37.163 42.935 27.079 1.00 25.46 N ATOM 4315 CZARG B 592 36.913 42.861 25.781 1.00 24.58 C ATOM 4316 NH1 ARG B 59237.446 41.880 25.069 1.00 25.78 N ATOM 4317 NH2 ARG B 592 36.127 43.76025.206 1.00 26.82 N ATOM 4318 C ARG B 592 35.326 42.323 32.039 1.0025.35 C ATOM 4319 O ARG B 592 34.803 43.415 32.284 1.00 25.98 O ATOM4320 N MET B 593 34.722 41.165 32.293 1.00 23.15 N ATOM 4321 CA MET B593 33.380 41.176 32.867 1.00 24.63 C ATOM 4322 CB MET B 593 32.77439.764 32.822 1.00 22.51 C ATOM 4323 CG MET B 593 31.324 39.697 33.2181.00 22.94 C ATOM 4324 SD MET B 593 30.230 10.679 32.086 1.00 29.24 SATOM 4325 CE MET B 593 29.463 41.710 33.269 1.00 27.63 C ATOM 4326 C METB 593 33.442 41.705 34.297 1.00 25.96 C ATOM 4327 O MET B 593 32.58242.480 34.719 1.00 28.48 O ATOM 4328 N ARG B 594 34.459 41.296 35.0441.00 23.96 N ATOM 4329 CA ARG B 594 34.605 41.743 36.417 1.00 24.96 CATOM 4330 CB ARG B 594 35.849 41.106 37.042 1.00 23.17 C ATOM 4331 CGARG B 594 36.061 41.480 38.522 1.00 25.85 C ATOM 4332 CD ARG B 59437.401 40.946 39.044 1.00 37.38 C ATOM 4333 NE ARG B 594 37.415 39.49039.157 1.00 42.96 N ATOM 4334 CZ ARG B 594 36.932 38.814 40.201 1.0043.14 C ATOM 4335 NH1 ARG B 594 36.400 39.464 41.232 1.00 47.77 N ATOM4336 NH2 ARG B 594 36.966 37.488 40.206 1.00 41.23 N ATOM 4337 C ARG B594 34.707 43.271 36.461 1.00 27.20 C ATOM 4338 O ARG B 594 34.07143.930 37.291 1.00 29.00 O ATOM 4339 N ALA B 595 35.499 43.827 35.5481.00 29.98 N ATOM 4340 CA ALA B 595 35.709 45.271 35.455 1.00 32.90 CATOM 4341 CB ALA B 595 36.814 45.570 34.424 1.00 33.21 C ATOM 4342 C ALAB 595 34.423 46.010 35.087 1.00 33.52 C ATOM 4343 O ALA B 595 34.13947.075 35.627 1.00 31.72 O ATOM 4344 N CYS B 596 33.646 45.439 34.1661.00 31.09 N ATOM 4345 CA CYS B 596 32.389 46.044 33.750 1.00 32.73 CATOM 4346 CB CYS B 596 31.768 45.264 32.585 1.00 31.31 C ATOM 4347 SGCYS B 596 32.614 45.490 30.999 1.00 41.27 S ATOM 4348 C CYS B 596 31.41246.053 34.907 1.00 33.26 C ATOM 4349 O CYS B 596 30.741 47.055 35.1581.00 31.15 O ATOM 4350 N TYR B 597 31.326 44.925 35.604 1.00 28.78 NATOM 4351 CA TYR B 597 30.415 44.811 36.736 1.00 29.03 C ATOM 4352 CBTYR B 597 30.465 43.384 37.311 1.00 30.58 C ATOM 4353 CG TYR B 59729.811 43.233 38.665 1.00 31.39 C ATOM 4354 CD1 TYR B 597 28.548 43.77338.917 1.00 33.23 C ATOM 4355 CE1 TYR B 597 27.957 43.673 40.186 1.0036.25 C ATOM 4356 CD2 TYR B 597 30.465 42.579 39.702 1.00 36.29 C ATOM4357 CE2 TYR B 597 29.884 42.466 40.977 1.00 42.36 C ATOM 4358 CZ TYR B597 28.634 43.021 41.210 1.00 40.23 C ATOM 4359 OH TYR B 597 28.09142.957 42.474 1.00 40.28 O ATOM 4360 C TYR B 597 30.758 45.825 37.8271.00 32.53 C ATOM 4361 O TYR B 597 29.871 46.537 38.335 1.00 33.59 OATOM 4362 N TYR B 598 32.036 45.883 38.179 1.00 30.77 N ATOM 4363 CA TYRB 598 32.508 46.793 39.218 1.00 38.97 C ATOM 4364 CB TYR B 598 34.01246.604 39.460 1.00 39.06 C ATOM 4365 CG TYR B 598 34.385 45.365 40.2441.00 40.81 C ATOM 4366 CD1 TYR B 598 35.714 45.111 40.590 1.00 48.71 CATOM 4367 CE1 TYR B 598 36.075 43.943 41.281 1.00 48.51 C ATOM 4368 CD2TYR B 598 33.424 44.423 40.612 1.00 47.38 C ATOM 4369 CE2 TYR B 59833.771 43.259 41.298 1.00 46.97 C ATOM 4370 CZ TYR B 598 35.098 43.02441.626 1.00 49.34 C ATOM 4371 OH TYR B 598 32.445 41.854 42.264 1.0048.67 O ATOM 4372 C TYR B 598 32.227 48.230 38.823 1.00 43.37 C ATOM4373 O TYR B 598 31.873 49.057 39.667 1.00 48.95 O ATOM 4374 N SER B 59932.379 48.535 37.541 1.00 37.43 N ATOM 4375 CA SER B 599 32.122 49.87237.055 1.00 43.16 C ATOM 4376 CB SER B 599 32.529 49.961 35.590 1.0043.45 C ATOM 4377 OG SER B 599 32.332 51.262 35.090 1.00 53.97 O ATOM4378 C SER B 599 30.636 50.205 37.223 1.00 45.93 C ATOM 4379 O SER B 59930.271 51.316 37.617 1.00 40.00 O ATOM 4380 N LEU B 600 29.773 49.24036.935 1.00 39.11 N ATOM 4381 CA LEU B 600 28.337 49.462 37.065 1.0044.57 C ATOM 4382 CB LEU B 600 27.552 48.395 36.295 1.00 38.25 C ATOM4383 CG LEU B 600 27.711 48.411 34.770 1.00 42.03 C ATOM 4384 CD1 LEU B600 27.111 47.196 34.147 1.00 37.50 C ATOM 4385 CD2 LEU B 600 27.03949.683 34.214 1.00 45.85 C ATOM 4386 C LEU B 600 27.897 49.456 38.5161.00 43.73 C ATOM 4387 O LEU B 600 26.980 50.191 38.892 1.00 46.87 OATOM 4388 N ALA B 601 28.556 48.628 39.323 1.00 40.69 N ATOM 4389 CA ALAB 601 28.242 48.478 40.741 1.00 47.37 C ATOM 4390 CB ALA B 601 29.06547.346 41.335 1.00 46.75 C ATOM 4391 C ALA B 601 28.506 49.775 41.4981.00 52.65 C ATOM 4392 O ALA B 601 27.834 50.082 42.483 1.00 53.31 OATOM 4393 N SER B 602 29.492 50.527 41.021 1.00 52.09 N ATOM 4394 CA SERB 602 29.860 51.804 41.617 1.00 57.33 C ATOM 4395 CB SER B 602 31.34652.069 41.381 1.00 58.94 C ATOM 4396 OG SER B 602 32.141 51.082 42.0201.00 59.82 O ATOM 4397 C SER B 602 29.024 52.912 40.981 1.00 59.94 CATOM 4398 O SER B 602 29.388 54.086 41.029 1.00 64.66 O ATOM 4399 N LYSB 603 27.900 52.515 40.389 1.00 62.33 N ATOM 4400 CA LYS B 603 26.97453.425 39.720 1.00 64.02 C ATOM 4401 CB LYS B 603 26.569 54.555 40.6731.00 64.16 C ATOM 4402 CG LYS B 603 25.091 54.908 40.626 1.00 65.22 CATOM 4403 CD LYS B 603 24.767 55.995 41.635 1.00 64.28 C ATOM 4404 CELYS B 603 23.270 56.270 41.693 1.00 67.89 C ATOM 4405 NZ LYS B 60322.949 57.422 42.589 1.00 67.06 N ATOM 4406 C LYS B 603 27.609 53.99638.446 1.00 65.47 C ATOM 4407 O LYS B 603 27.032 53.798 37.352 1.0066.51 O ATOM 4408 OXT LYS B 603 28.682 54.625 38.551 1.00 68.34 O TER 1LYS B 603 ATOM 4409 O4 STU C 995 10.701 −7.072 −3.088 1.00 26.93 O ATOM4410 C25 STU C 995 11.180 −5.863 −3.690 1.00 23.34 C ATOM 4411 C24 STU C995 10.859 −4.664 −2.680 1.00 29.45 C ATOM 4412 C23 STU C 995 10.138−5.127 −1.364 1.00 22.89 C ATOM 4413 C22 STU C 995 8.878 −5.986 −1.6971.00 25.16 C ATOM 4414 C21 STU C 995 9.461 −7.275 −2.433 1.00 26.44 CATOM 4415 C26 STU C 995 9.777 −8.334 −1.360 1.00 25.18 C ATOM 4416 N2STU C 995 8.422 −7.719 −3.422 1.00 23.09 N ATOM 4417 C18 STU C 995 8.412−7.138 −4.747 1.00 21.71 C ATOM 4418 C19 STU C 995 9.290 −6.274 −6.4051.00 24.08 C ATOM 4419 C6 STU C 995 9.064 −5.832 −6.736 1.00 22.57 CATOM 4420 C7 STU C 995 7.866 −6.422 −7.405 1.00 25.97 C ATOM 4421 C10STU C 995 7.050 −7.293 −6.788 1.00 23.03 C ATOM 4422 C11 STU C 995 7.275−7.726 −5.438 1.00 20.70 C ATOM 4423 C12 STU C 995 6.603 −8.591 −4.5231.00 24.72 C ATOM 4424 C17 STU C 995 7.298 −8.588 −3.264 1.00 25.22 CATOM 4425 C16 STU C 995 6.820 −9.373 −2.193 1.00 26.63 C ATOM 4426 C15STU C 995 5.671 −10.131 −2.193 1.00 26.63 C ATOM 4427 C14 STU C 9954.957 −10.136 −3.585 1.00 27.59 C ATOM 4428 C13 STU C 995 5.443 −9.364−4.643 1.00 24.26 C ATOM 4429 C9 STU C 995 5.906 −7.701 −7.728 1.0024.26 C ATOM 4430 N1 STU C 995 6.283 −6.914 −8.894 1.00 26.80 N ATOM4431 C8 STU C 995 7.390 −6.161 −8.794 1.00 24.42 C ATOM 4432 O5 STU C995 7.870 −5.431 −9.638 1.00 25.22 O ATOM 4433 C5 STU C 995 10.084−4.899 −7.090 1.00 21.94 C ATOM 4434 C20 STU C 995 10.927 −4.761 −5.9431.00 28.12 C ATOM 4435 C1 STU C 995 12.071 −3.894 −5.922 1.00 27.73 CATOM 4436 C2 STU C 995 12.350 −3.175 −7.097 1.00 30.27 C ATOM 4437 C3STU C 995 11.500 −3.313 −8.263 1.00 28.96 C ATOM 4438 C4 STU C 99510.403 −4.161 −8.243 1.00 26.89 C ATOM 4439 N3 STU C 995 10.433 −5.565−4.940 1.00 23.33 N ATOM 4440 O6 STU C 995 8.116 −5.181 −2.652 1.0024.62 O ATOM 4441 C27 STU C 995 6.704 −5.144 −2.385 1.00 24.32 C ATOM4442 N4 STU C 995 9.777 −3.833 −0.560 1.00 24.88 N ATOM 4443 C28 STU C995 9.296 −4.199 0.820 1.00 26.60 C TER 1 STU C 995 ATOM 4444 O4 STU D996 14.841 21.718 34.032 1.00 26.13 O ATOM 4445 C25 STU D 996 14.37322.920 34.632 1.00 22.93 C ATOM 4446 C24 STU D 996 14.706 24.128 33.6101.00 28.10 C ATOM 4447 C23 STU D 996 15.417 23.644 32.288 1.00 24.94 CATOM 4448 C22 STU D 996 16.665 22.776 32.631 1.00 23.21 C ATOM 4449 C21STU D 996 16.072 21.495 33.377 1.00 27.43 C ATOM 4450 C26 STU D 99615.756 20.434 32.323 1.00 26.04 C ATOM 4451 N2 STU D 996 17.133 21.07732.323 1.00 21.43 N ATOM 4452 C18 STU D 996 17.120 21.637 35.688 1.0020.69 C ATOM 4453 C19 STU D 996 16.275 22.524 36.330 1.00 23.53 C ATOM4454 C6 STU D 996 16.487 22.957 37.663 1.00 22.38 C ATOM 4455 C7 STU D996 17.682 22.366 38.337 1.00 26.78 C ATOM 4456 C10 STU D 996 18.50421.518 37.720 1.00 22.89 C ATOM 4457 C11 STU D 996 18.270 21.070 36.3701.00 19.86 C ATOM 4458 C12 STU D 996 18.952 20.227 35.457 1.00 22.51 CATOM 4459 C17 STU D 996 18.237 20.202 34.206 1.00 25.41 C ATOM 4460 C16STU D 996 18.719 19.424 33.133 1.00 26.19 C ATOM 4461 C15 STU D 99619.869 18.670 33.275 1.00 25.48 C ATOM 4462 C14 STU D 996 20.600 18.67834.521 1.00 25.48 C ATOM 4463 C13 STU D 996 20.112 19.449 35.580 1.0023.07 C ATOM 4464 C9 STU D 996 19.647 21.104 38.659 1.00 23.46 C ATOM4465 N1 STU D 996 19.276 21.887 39.826 1.00 25.16 N ATOM 4466 C8 STU D996 18.166 22.640 39.728 1.00 22.97 C ATOM 4467 O5 STU D 996 17.68823.365 40.576 1.00 23.93 O ATOM 4468 C5 STU D 996 15.472 23.870 38.0151.00 23.02 C ATOM 4469 C20 STU D 996 14.631 24.010 36.865 1.00 26.41 CATOM 4470 C1 STU D 996 13.476 24.883 36.850 1.00 25.65 C ATOM 4471 C2STU D 996 13.208 25.595 38.019 1.00 30.69 C ATOM 4472 C3 STU D 99614.057 25.459 39.181 1.00 27.27 C ATOM 4473 C4 STU D 996 15.157 24.61239.158 1.00 26.75 C ATOM 4474 N3 STU D 996 15.112 23.212 35.878 1.0022.92 N ATOM 4475 O6 STU D 996 17.429 23.573 33.576 1.00 23.16 O ATOM4476 C27 STU D 996 18.832 23.642 33.286 1.00 24.37 C ATOM 4477 N4 STU D996 15.802 24.935 31.463 1.00 23.94 N ATOM 4478 C28 STU D 996 16.27524.547 30.090 1.00 24.01 C TER 1 STU D 996 ATOM 4479 OH2 TIP S 1 0.4214.204 13.673 1.00 22.10 O ATOM 4480 OH2 TIP S 2 0.033 9.184 13.707 1.0021.18 O ATOM 4481 OH2 TIP S 3 11.945 −2.213 0.210 1.00 22.87 O ATOM 4482OH2 TIP S 4 25.132 33.017 17.239 1.00 22.45 O ATOM 4483 OH2 TIP S 525.496 37.992 17.154 1.00 20.79 O ATOM 4484 OH2 TIP S 6 −12.049 −13.94412.451 1.00 22.33 O ATOM 4485 OH2 TIP S 7 14.395 8.858 57.889 1.00 29.61O ATOM 4486 OH2 TIP S 8 13.627 26.578 30.735 1.00 22.89 O ATOM 4487 OH2TIP S 9 11.059 −19.955 −26.913 1.00 28.80 O ATOM 4488 OH2 TIP S 1029.070 27.910 20.630 1.00 25.77 O ATOM 4489 OH2 TIP S 11 −3.520 −0.80910.277 1.00 25.06 O ATOM 4490 OH2 TIP S 12 18.345 30.239 26.486 1.0023.39 O ATOM 4491 OH2 TIP S 13 1.869 14.815 18.471 1.00 23.60 O ATOM4492 OH2 TIP S 14 35.075 25.727 25.589 1.00 28.87 O ATOM 4493 OH2 TIP S15 7.227 1.385 4.419 1.00 22.68 O ATOM 4494 OH2 TIP S 16 −9.560 −3.0262.397 1.00 27.48 O ATOM 4495 OH2 TIP S 17 −5.464 −3.857 7.924 1.00 23.68O ATOM 4496 OH2 TIP S 18 −6.496 8.745 20.202 1.00 23.82 O ATOM 4497 OH2TIP S 19 −2.873 −2.292 5.603 1.00 23.16 O ATOM 4498 OH2 TIP S 20 −11.8038.285 18.254 1.00 24.29 O ATOM 4499 OH2 TIP S 21 28.416 26.453 25.2901.00 23.25 O ATOM 4500 OH2 TIP S 22 37.391 37.035 12.669 1.00 26.06 OATOM 4501 OH2 TIP S 23 −17.573 −7.098 4.343 1.00 27.79 O ATOM 4502 OH2TIP S 24 32.073 37.514 10.731 1.00 24.94 O ATOM 4503 OH2 TIP S 25 13.48031.449 36.563 1.00 25.71 O ATOM 4504 OH2 TIP S 26 −14.437 9.362 17.7301.00 32.36 O ATOM 4505 OH2 TIP S 27 35.416 25.457 18.662 1.00 25.28 OATOM 4506 OH2 TIP S 28 31.029 24.811 22.942 1.00 25.60 O ATOM 4507 OH2TIP S 29 −9.872 −3.294 12.263 1.00 24.74 O ATOM 4508 OH2 TIP S 30 26.4679.752 17.607 1.00 27.17 O ATOM 4509 OH2 TIP S 31 6.790 −6.857 1.076 1.0030.39 O ATOM 4510 OH2 TIP S 32 40.010 38.095 13.209 1.00 33.16 O ATOM4511 OH2 TIP S 33 34.735 13.425 28.194 1.00 29.80 O ATOM 4512 OH2 TIP S34 −9.205 −15.364 2.764 1.00 26.99 O ATOM 4513 OH2 TIP S 35 −0.980−18.986 13.270 1.00 26.43 O ATOM 4514 OH2 TIP S 36 24.213 18.114 34.6941.00 29.43 O ATOM 4515 OH2 TIP S 37 1.416 −10.764 −3.798 1.00 29.81 OATOM 4516 OH2 TIP S 38 43.144 21.699 26.548 1.00 30.26 O ATOM 4517 OH2TIP S 39 −14.848 7.171 −3.854 1.00 30.65 O ATOM 4518 OH2 TIP S 40 39.18042.936 36.141 1.00 31.31 O ATOM 4519 OH2 TIP S 41 40.406 35.919 34.7481.00 30.00 O ATOM 4520 OH2 TIP S 42 0.420 2.218 15.485 1.00 29.77 O ATOM4521 OH2 TIP S 43 35.271 29.926 13.265 1.00 31.24 O ATOM 4522 OH2 TIP S44 12.095 2.647 −5.592 1.00 26.76 O ATOM 4523 OH2 TIP S 45 −9.718 1.17217.653 1.00 30.07 O ATOM 4524 OH2 TIP S 46 −3.404 14.594 13.732 1.0030.39 O ATOM 4525 OH2 TIP S 47 18.726 21.922 29.867 1.00 32.07 O ATOM4526 OH2 TIP S 48 13.555 7.866 51.920 1.00 39.23 O ATOM 4527 OH2 TIP S49 28.975 43.404 17.200 1.00 29.02 O ATOM 4528 OH2 TIP S 50 −13.56914.156 −5.246 1.00 33.70 O ATOM 4528 OH2 TIP S 51 26.355 20.255 28.8321.00 29.58 O ATOM 4530 OH2 TIP S 52 9.161 10.323 16.585 1.00 35.40 OATOM 4531 OH2 TIP S 53 −0.757 −8.626 2.106 1.00 29.81 O ATOM 4532 OH2TIP S 54 −14.070 −4.107 6.620 1.00 27.24 O ATOM 4533 OH2 TIP S 55 11.946−20.893 −21.008 1.00 43.13 O ATOM 4534 OH2 TIP S 56 25.189 30.969 15.4541.00 29.79 O ATOM 4535 OH2 TIP S 57 36.813 31.260 38.289 1.00 31.14 OATOM 4536 OH2 TIP S 58 −11.290 2.441 −7.391 1.00 30.15 O ATOM 4537 OH2TIP S 59 9.218 10.129 12.339 1.00 32.37 O ATOM 4538 OH2 TIP S 60 16.46939.110 14.335 1.00 36.98 O ATOM 4539 OH2 TIP S 61 39.600 24.658 24.3471.00 28.57 O ATOM 4540 OH2 TIP S 62 40.886 19.814 39.523 1.00 31.30 OATOM 4541 OH2 TIP S 63 28.663 25.506 21.907 1.00 28.05 O ATOM 4542 OH2TIP S 64 16.334 39.034 18.587 1.00 30.97 O ATOM 4543 OH2 TIP S 65 −4.453−10.056 −10.600 1.00 35.01 O ATOM 4544 OH2 TIP S 66 30.644 48.610 22.3381.00 34.83 O ATOM 4545 OH2 TIP S 67 29.080 17.008 23.184 1.00 42.53 OATOM 4546 OH2 TIP S 68 20.437 −8.985 −8.586 1.00 30.66 O ATOM 4547 OH2TIP S 69 −3.136 −3.317 8.937 1.00 26.92 O ATOM 4548 OH2 TIP S 70 −3.528−11.754 7.661 1.00 42.36 O ATOM 4549 OH2 TIP S 71 −14.052 9.990 −6.7841.00 36.91 O ATOM 4550 OH2 TIP S 72 13.280 20.389 48.150 1.00 37.12 OATOM 4551 OH2 TIP S 73 39.598 27.291 23.321 1.00 29.86 O ATOM 4552 OH2TIP S 74 −14.000 −1.419 7.609 1.00 29.52 O ATOM 4553 OH2 TIP S 75 12.287−8.370 −17.212 1.00 38.16 O ATOM 4554 OH2 TIP S 76 0.127 −2.062 7.3361.00 31.92 O ATOM 4555 OH2 TIP S 77 39.657 38.747 37.688 1.00 35.97 OATOM 4556 OH2 TIP S 78 6.921 10.871 13.240 1.00 39.95 O ATOM 4557 OH2TIP S 79 3.173 20.739 −5.925 1.00 36.12 O ATOM 4558 OH2 TIP S 80 2.499−2.849 7.192 1.00 37.12 O ATOM 4559 OH2 TIP S 81 −5.087 20.010 8.5851.00 36.89 O ATOM 4560 OH2 TIP S 82 25.391 26.672 23.460 1.00 34.04 OATOM 4561 OH2 TIP S 83 23.029 25.932 23.668 1.00 37.18 O ATOM 4562 OH2TIP S 84 13.382 −6.941 −0.286 1.00 40.85 O ATOM 4563 OH2 TIP S 85 27.71512.569 29.074 1.00 44.29 O ATOM 4564 OH2 TIP S 86 29.990 18.665 41.4911.00 37.50 O ATOM 4565 OH2 TIP S 87 22.380 47.448 36.934 1.00 39.98 OATOM 4566 OH2 TIP S 88 18.662 39.652 17.714 1.00 39.70 O ATOM 4567 OH2TIP S 89 40.100 17.469 30.708 1.00 36.01 O ATOM 4568 OH2 TIP S 90−14.239 11.528 5.631 1.00 40.89 O ATOM 4569 OH2 TIP S 91 15.281 18.93157.001 1.00 45.15 O ATOM 4570 OH2 TIP S 92 15.691 −4.194 −6.244 1.0046.89 O ATOM 4571 OH2 TIP S 93 −5.712 −9.326 5.564 1.00 28.37 O ATOM4572 OH2 TIP S 94 12.167 21.855 31.241 1.00 41.68 O ATOM 4573 OH2 TIP S95 −3.343 −17.247 16.589 1.00 36.78 O ATOM 4574 OH2 TIP S 96 11.15623.711 33.209 1.00 35.57 O ATOM 4575 OH2 TIP S 97 25.545 16.245 18.6211.00 42.42 O ATOM 4576 OH2 TIP S 98 40.918 18.920 34.722 1.00 45.15 OATOM 4577 OH2 TIP S 99 11.862 37.569 22.369 1.00 39.52 O ATOM 4578 OH2TIP S 100 15.658 8.162 −3.968 1.00 36.43 O ATOM 4579 OH2 TIP S 101 9.90224.553 37.142 1.00 45.39 O ATOM 4580 OH2 TIP S 102 6.314 −5.317 −19.6521.00 42.39 O ATOM 4581 OH2 TIP S 103 41.337 39.304 18.249 1.00 43.68 OATOM 4582 OH2 TIP S 104 1.800 −8.520 −5.551 1.00 35.38 O ATOM 4583 OH2TIP S 105 −2.162 −16.185 1.874 1.00 43.33 O ATOM 4584 OH2 TIP S 10639.849 40.296 25.274 1.00 39.96 O ATOM 4585 OH2 TIP S 107 17.812 14.37726.537 1.00 49.82 O ATOM 4586 OH2 TIP S 108 20.087 16.149 58.833 1.0041.90 O ATOM 4587 OH2 TIP S 109 23.681 20.283 36.450 1.00 34.15 O ATOM4588 OH2 TIP S 110 31.232 19.396 25.383 1.00 31.15 O ATOM 4589 OH2 TIP S111 9.926 36.917 34.935 1.00 39.68 O ATOM 4590 OH2 TIP S 112 13.7428.657 8.468 1.00 37.13 O ATOM 4591 OH2 TIP S 113 14.444 −5.155 −2.3321.00 34.36 O ATOM 4592 OH2 TIP S 114 −14.505 −11.350 0.205 1.00 38.40 OATOM 4593 OH2 TIP S 115 −14.458 0.142 5.499 1.00 35.12 O ATOM 4594 OH2TIP S 116 −0.021 −12.439 12.153 1.00 43.53 O ATOM 4595 OH2 TIP S 11728.916 11.485 14.387 1.00 40.27 O ATOM 4596 OH2 TIP S 118 −4.527 10.289−9.542 1.00 45.18 O ATOM 4597 OH2 TIP S 119 1.974 14.755 −11.306 1.0047.77 O ATOM 4598 OH2 TIP S 120 −15.749 10.668 12.672 1.00 45.53 O ATOM4599 OH2 TIP S 121 −11.214 −2.226 −11.345 1.00 46.10 O ATOM 4600 OH2 TIPS 122 36.682 45.523 28.569 1.00 37.78 O ATOM 4601 OH2 TIP S 123 19.32023.480 50.684 1.00 40.47 O ATOM 4602 OH2 TIP S 124 −15.435 −9.919 −3.8111.00 41.21 O ATOM 4603 OH2 TIP S 125 38.588 26.717 13.793 1.00 44.52 OATOM 4604 OH2 TIP S 126 7.685 −14.424 4.306 1.00 51.58 O ATOM 4605 OH2TIP S 127 36.734 26.561 42.263 1.00 44.35 O ATOM 4606 OH2 TIP S 12823.012 18.699 64.427 1.00 55.43 O ATOM 4607 OH2 TIP S 129 −11.079 16.7532.337 1.00 36.15 O ATOM 4608 OH2 TIP S 130 32.804 36.247 8.025 1.0046.53 O ATOM 4609 OH2 TIP S 131 5.452 −12.666 −27.857 1.00 46.53 O ATOM4610 OH2 TIP S 132 5.777 −5.213 4.878 1.00 52.94 O ATOM 4611 OH2 TIP S133 17.902 43.584 22.88 1.00 38.79 O ATOM 4612 OH2 TIP S 134 41.52941.359 30.489 1.00 45.08 O ATOM 4613 OH2 TIP S 135 19.433 49.428 35.0711.00 36.73 O ATOM 4614 OH2 TIP S 136 40.681 17.939 17.861 1.00 52.60 OATOM 4615 OH2 TIP S 137 7.694 14.779 8.016 1.00 38.37 O ATOM 4616 OH2TIP S 138 43.631 21.569 35.087 1.00 42.92 O ATOM 4617 OH2 TIP S 139−14.096 −4.522 2.725 1.00 38.87 O ATOM 4618 OH2 TIP S 140 39.647 24.35728.138 1.00 37.44 O ATOM 4619 OH2 TIP S 141 34.792 45.810 26.786 1.0033.97 O ATOM 4620 OH2 TIP S 142 35.678 30.939 40.741 1.00 50.18 O ATOM4621 OH2 TIP S 143 1.690 −5.943 7.932 1.00 46.04 O ATOM 4622 OH2 TIP S144 16.446 8.323 29.203 1.00 43.29 O ATOM 4623 OH2 TIP S 145 4.806−6.139 −16.268 1.00 46.89 O ATOM 4624 OH2 TIP S 146 9.706 7.514 −13.8471.00 40.39 O ATOM 4625 OH2 TIP S 147 −2.757 −8.476 20.990 1.00 44.56 OATOM 4626 OH2 TIP S 148 19.924 51.030 32.912 1.00 56.09 O ATOM 4627 OH2TIP S 149 −9.256 17.012 4.187 1.00 37.40 O ATOM 4628 OH2 TIP S 15013.798 12.721 1.801 1.00 41.15 O ATOM 4629 OH2 TIP S 151 −16.062 12.5220.503 1.00 45.91 O ATOM 4630 OH2 TIP S 152 43.042 24.814 30.118 1.0045.63 O ATOM 4631 OH2 TIP S 153 32.777 49.012 32.108 1.00 49.84 O ATOM4632 OH2 TIP S 154 35.924 45.614 31.001 1.00 42.83 O ATOM 4633 OH2 TIP S155 −4.339 −23.117 −0.551 1.00 49.33 O ATOM 4634 OH2 TIP S 156 19.82723.697 25.905 1.00 53.14 O ATOM 4635 OH2 TIP S 157 37.820 44.919 22.1451.00 44.38 O ATOM 4636 OH2 TIP S 158 40.593 29.995 32.300 1.00 31.52 OATOM 4637 OH2 TIP S 159 −15.055 1.168 −1.359 1.00 30.62 O ATOM 4638 OH2TIP S 160 −16.412 7.003 5.433 1.00 32.94 O ATOM 4639 OH2 TIP S 16115.985 29.616 25.353 1.00 32.94 O ATOM 4640 OH2 TIP S 162 42.076 35.83225.453 1.00 35.51 O ATOM 4641 OH2 TIP S 163 10.339 −9.751 −25.987 1.0046.65 O ATOM 4642 OH2 TIP S 164 34.356 38.780 10.727 1.00 36.90 O ATOM4643 OH2 TIP S 165 9.618 0.824 5.500 1.00 35.38 O ATOM 4644 OH2 TIP S166 26.940 9.884 20.217 1.00 38.88 O ATOM 4645 OH2 TIP S 167 −7.0237.631 22.982 1.00 45.13 O ATOM 4646 OH2 TIP S 168 −17.523 −3.768 0.7641.00 47.38 O ATOM 4647 OH2 TIP S 169 34.610 28.019 11.023 1.00 41.98 OATOM 4648 OH2 TIP S 170 38.500 22.241 10.888 1.00 49.86 O ATOM 4649 OH2TIP S 171 39.773 16.186 22.302 1.00 42.81 O ATOM 4650 OH2 TIP S 17239.007 29.639 38.711 1.00 40.01 O ATOM 4651 OH2 TIP S 173 −3.162 −13.9721.056 1.00 37.80 O ATOM 4652 OH2 TIP S 174 15.866 36.292 44.854 1.0041.03 O ATOM 4653 OH2 TIP S 175 28.716 14.934 29.871 1.00 40.86 O ATOM4654 OH2 TIP S 176 12.877 7.462 40.598 1.00 50.68 O ATOM 4655 OH2 TIP S177 6.133 20.704 −4.054 1.00 39.16 O ATOM 4656 OH2 TIP S 178 39.96928.942 25.391 1.00 38.15 O ATOM 4657 OH2 TIP S 179 −13.449 0.920 −7.6681.00 44.30 O ATOM 4658 OH2 TIP S 180 1.907 −19.850 −13.019 1.00 46.61 OATOM 4659 OH2 TIP S 181 −11.803 7.776 20.873 1.00 44.08 O ATOM 4660 OH2TIP S 182 15.943 16.779 25.867 1.00 50.71 O ATOM 4661 OH2 TIP S 18311.887 41.459 29.150 1.00 40.31 O ATOM 4662 OH2 TIP S 184 −12.916 −6.60420.001 1.00 48.89 O ATOM 4663 OH2 TIP S 185 37.386 36.717 10.040 1.0047.31 O ATOM 4664 OH2 TIP S 186 2.834 18.279 41.221 1.00 54.64 O ATOM4665 OH2 TIP S 187 −9.066 −0.690 19.812 1.00 43.53 O ATOM 4666 OH2 TIP S188 16.454 33.980 25.756 1.00 38.52 O ATOM 4667 OH2 TIP S 189 23.85122.769 22.843 1.00 48.45 O ATOM 4668 OH2 TIP S 190 −14.255 −12.614 8.7731.00 46.74 O ATOM 4669 OH2 TIP S 191 −5.249 −12.948 −12.695 1.00 53.90 OATOM 4670 OH2 TIP S 192 9.039 −20.611 1.774 1.00 42.77 O ATOM 4671 OH2TIP S 193 −5.304 −5.892 −10.918 1.00 47.95 O ATOM 4672 OH2 TIP S 1949.516 −11.723 5.016 1.00 49.40 O ATOM 4673 OH2 TIP S 195 20.372 36.2656.690 1.00 42.55 O ATOM 4674 OH2 TIP S 196 9.099 5.271 5.043 1.00 40.29O ATOM 4675 OH2 TIP S 197 28.290 20.438 9.887 1.00 44.18 O ATOM 4676 OH2TIP S 198 41.403 24.242 26.360 1.00 41.99 O ATOM 4677 OH2 TIP S 19917.555 −7.280 −3.972 1.00 45.72 O ATOM 4678 OH2 TIP S 200 11.643 26.38733.558 1.00 44.67 O ATOM 4679 OH2 TIP S 201 −13.080 −2.043 17.068 1.0048.89 O ATOM 4680 OH2 TIP S 202 21.406 41.180 6.510 1.00 47.83 O ATOM4681 OH2 TIP S 203 −3.647 −14.349 4.372 1.00 45.03 O ATOM 4682 OH2 TIP S204 1.975 −16.444 0.528 1.00 46.05 O ATOM 4683 OH2 TIP S 205 29.35238.318 42.802 1.00 39.18 O ATOM 4684 OH2 TIP S 206 23.716 43.491 42.2181.00 52.21 O ATOM 4685 OH2 TIP S 207 37.832 29.664 12.655 1.00 40.31 OATOM 4686 OH2 TIP S 208 4.964 17.602 2.226 1.00 49.67 O ATOM 4687 OH2TIP S 209 39.168 40.024 22.519 1.00 48.01 O ATOM 4688 OH2 TIP S 21013.868 −18.464 −3.462 1.00 45.96 O ATOM 4689 OH2 TIP S 211 −15.848−4.527 4.594 1.00 44.75 O ATOM 4690 OH2 TIP S 212 −10.372 16.898 −0.0551.00 41.74 O ATOM 4691 OH2 TIP S 213 −3.769 9.428 −11.859 1.00 41.64 OATOM 4692 OH2 TIP S 214 −12.248 16.128 8.702 1.00 42.97 O ATOM 4693 OH2TIP S 215 −10.705 −1.226 −13.945 1.00 46.83 O ATOM 4694 OH2 TIP S 21622.402 4.106 44.758 1.00 42.90 O ATOM 4695 OH2 TIP S 217 −17.355 1.2651.310 1.00 49.40 O ATOM 4696 OH2 TIP S 218 42.477 37.616 23.340 1.0042.07 O ATOM 4697 OH2 TIP S 219 −16.918 8.816 7.795 1.00 46.92 O ATOM4698 OH2 TIP S 220 27.500 8.859 43.884 1.00 48.46 O ATOM 4699 OH2 TIP S221 30.021 39.029 40.447 1.00 44.55 O ATOM 4700 OH2 TIP S 222 39.39118.850 37.190 1.00 52.09 O ATOM 4701 OH2 TIP S 223 4.533 −18.856 1.9221.00 50.69 O ATOM 4702 OH2 TIP S 224 29.183 14.389 26.673 1.00 47.97 OATOM 4703 OH2 TIP S 225 −18.903 −8.822 10.919 1.00 49.49 O ATOM 4704 OH2TIP S 226 29.080 14.271 21.460 1.00 41.94 O ATOM 4705 OH2 TIP S 227−12.418 15.936 −7.420 1.00 49.12 O ATOM 4706 OH2 TIP S 228 40.908 38.79810.820 1.00 48.24 O ATOM 4707 OH2 TIP S 229 20.873 22.585 47.103 1.0050.53 O ATOM 4708 OH2 TIP S 230 21.831 −10.033 −6.237 1.00 53.05 O ATOM4709 OH2 TIP S 231 29.823 5.586 31.413 1.00 52.07 O ATOM 4710 OH2 TIP S232 44.472 19.890 19.952 1.00 49.75 O ATOM 4711 OH2 TIP S 233 −14.590−13.479 12.084 1.00 44.70 O ATOM 4712 OH2 TIP S 234 36.315 29.168 8.5981.00 49.27 O ATOM 4713 OH2 TIP S 235 −3.492 −14.586 9.423 1.00 44.24 OATOM 4714 OH2 TIP S 236 37.931 44.730 38.212 1.00 52.70 O ATOM 4715 OH2TIP S 237 −13.540 11.244 8.565 1.00 48.15 O ATOM 4716 OH2 TIP S 238−15.408 10.000 20.145 1.00 50.07 O ATOM 4717 OH2 TIP S 239 20.743 2.60848.382 1.00 49.86 O ATOM 4718 OH2 TIP S 240 23.597 12.310 30.357 1.0048.72 O ATOM 4719 OH2 TIP S 241 −5.755 −8.661 −12.899 1.00 51.10 O ATOM4720 OH2 TIP S 242 40.644 44.705 34.483 1.00 51.24 O ATOM 4721 OH2 TIP S243 32.880 11.239 31.811 1.00 48.34 O ATOM 4722 OH2 TIP S 244 −7.454−17.415 −0.915 1.00 45.03 O ATOM 4723 OH2 TIP S 245 13.922 −2.398 −2.5041.00 46.83 O ATOM 4724 OH2 TIP S 246 0.782 12.427 −14.770 1.00 48.57 OATOM 4725 OH2 TIP S 247 −15.049 15.812 −3.622 1.00 51.01 O ATOM 4726 OH2TIP S 248 4.404 15.313 18.746 1.00 47.05 O ATOM 4727 OH2 TIP S 24931.402 20.217 43.758 1.00 52.57 O ATOM 4728 OH2 TIP S 250 −10.062 2.073−9.809 1.00 50.33 O ATOM 4729 OH2 TIP S 251 11.650 −0.830 4.614 1.0050.82 O ATOM 4730 OH2 TIP S 252 −1.232 −15.435 4.563 1.00 50.12 O ATOM4731 OH2 TIP S 253 −12.330 0.786 18.255 1.00 43.46 O ATOM 4732 OH2 TIP S254 36.403 27.682 44.769 1.00 51.60 O ATOM 4733 OH2 TIP S 255 −18.2736.055 3.212 1.00 51.88 O ATOM 4734 OH2 TIP S 256 −13.609 16.893 −0.6321.00 50.05 O ATOM 4735 OH2 TIP S 257 14.001 15.235 0.255 1.00 48.29 OATOM 4736 OH2 TIP S 258 10.461 2.911 6.999 1.00 51.70 O ATOM 4737 OH2TIP S 259 11.740 10.308 34.387 1.00 49.96 O ATOM 4738 OH2 TIP S 260−11.901 5.018 −8.016 1.00 50.95 O ATOM 4739 OH2 TIP S 261 −10.492 19.957−5.817 1.00 45.58 O TER 1 TIP S 261 END

TABLE 2 Crystal Data and X-ray data statistics Number of crystals 1Space group P1 (primitive triclinic) Unit cell dimensions a = 35.77 b =57.56 c = 80.20 Å α = 68.97 β = 89.83 γ = 89.95° Number of monomers/a.u.2 Packing coefficient 2.05 Å³/Da Solvent content   38% Resolution range50-1.9 Å Number of observations 386926 Number of reject observations24465 Number of unique reflections 46855 Mosaicity 0.817 Overall Dataredundancy 8.25 Data completeness   97.0% <I/σ (I)> 20.6 R_(merge) 0.049Highest resolution shell Resolution range 1.97-1.90 Å Completeness forshell   96.5% R_(merge) for shell 0.175 Reflections with I ≧ 3σ(I)  86.7%

TABLE 3 Refinement Statistics Data used in refinement resolution range19.26-1.90 Å intensity cutoff (Sigma(F)) 0.0 number of reflections 45463completeness (working + test set)   96.7% test set    5.0% Fit to dataused in refinement overall R_(cryst) 0.182 overall R_(free) 0.209 Fit inthe highest resolution bin resolution range  2.02-1.90 Å bincompleteness (working + test set)   93.7% bin R_(cryst) 0.195 binR_(free) 0.241 Number of non-hydrogen atoms protein atoms 4478 ligand (2molecules staurosporin) 70 waters 261 Overall B value from Wilson plot  24.1 Å² Overall mean B value   35.0 Å² Cross-validated estimatedcoordinate error (low res. cutoff: 5.0 Å) from Luzzati plot  0.22 Å fromσ_(A)  0.11 Å Rms deviations from ideal values bond lengths   0.011 Åbond angles   1.3° dihedral angles  21.4° improper angles  0.91°

TABLE 4 List of Contacts Between Catalytic Domain of ZAP-70 andStaurosporine atom in protein atom in staurosporine distance (A) LEU 344O STU C25 3.4 GLY 345 CA STU O4 3.5 CYS 346 O STU C26 3.9 GLY 347 N STUC26 5.4 PHE 349 CZ STU C16 4.5 VAL 352 CG2 STU C17 3.8 ALA 367 CB STU N13.2 LYS 369 CD STU C14 4.3 GLU 386 OE2 STU C14 4.4 VAL 399 CG1 STU C94.1 MET 414 CE STU C13 3.6 GLU 415 O STU N1 3.0 H-bridge MET 416 CA STUO5 3.4 ALA 417 N STU O5 2.7 H-bridge GLY 418 O STU C3 4.3 GLY 419 C STUC3 4.8 GLY 420 CA STU C3 3.5 PRO 421 CG STU C24 3.8 HIS 423 NE2 STU N45.1 through Solv3 Lys 424 NZ STU N4 6.4 through Solv3 ARG 465 O STU N43.0 H-bridge ASN 466 OD1 STU C27 3.4 LEU 468 CD1 STU C7 3.3 SER 478 OGSTU C27 3.1 Alt. Pos. ASP 479 CG STU C15 3.5

1. A crystal of the ZAP-70 kinase comprising the catalytic domain ofZAP-70 kinase with a unit cell dimension of a=35.77±5 Ångstroms,b=57.56±5 Ångstroms, c=80.20±5 Ångstroms; α=68.97±5 degrees, β=89.83±5degrees, γ=89.95±5 degrees.
 2. A crystal of the ZAP-70 kinase comprisingthe catalytic domain of ZAP-70 kinase wherein said catalytic domain hasa three-dimensional structure comprising the atomic structurecoordinates of Table
 1. 3. A crystal of claim 1 wherein the catalyticdomain of ZAP-70 kinase comprises the sequence of SEQ ID. No. 2,fragment or a homologue thereof.
 4. A crystal of claim 3 wherein thecatalytic domain of ZAP-70 kinase comprises at least the ATP-bindingsite.
 5. A crystal of claim 1 bound to at least one ligand or lowmolecular weight compound.
 6. A computer readable medium comprising datastorage material encoded with computer readable data wherein said datacomprises the atomic coordinates of Table 1 comprising the catalyticdomain of ZAP-70 kinase.
 7. A method for making a crystal of a ZAP-70kinase comprising the steps of: (i) purification of the full-lengthZAP-70 kinase of SEQ ID No.1 (ii) proteolytic domain definition (iii)expression of the full-length ZAP-70 kinase of SEQ ID No.1 flanked byprotease recognition sequences to facilitate proteolytic release of thedesired domain of ZAP-70 (iv) expression of the full-length ZAP-70kinase of step (iii) in a suitable host cell (v) controlled proteolysisof the desired domain at protease recognition sites (vi) rapidpurification of the desired ZAP-70 domain.
 8. A method according toclaim 7 wherein the domain comprises the catalytic domain of ZAP-70kinase of SEQ ID No.2, fragment or a homologue thereof.
 9. A methodaccording to claim 7 wherein the catalytic domain of ZAP-70, fragment orhomologue thereof is bound to at least one ligand or low molecule weightchemical compound at any step prior to crystallization.
 10. A method ofdetermining the three-dimensional structure of the catalytic domain ofZAP-70 comprising: (i) crystallization of ZAP-70 kinase comprising thecatalytic domain of ZAP-70 (SEQ ID No.2), fragment or homologue thereof(ii) utilizing the atomic coordinates of Table 1 in whole or in part todetermine the three dimensional structure of the catalytic domain ofZAP-70, fragment or homologue thereof.
 11. A method for determining thethree-dimensional structure of a complex comprising the catalytic domainof ZAP-70 kinase (SEQ ID No.2), fragment or homologue thereof bound toat least one ligand comprising: (i) obtaining x-ray diffraction data forcrystals of the complex (ii) utilizing the atomic coordinates of Table 1in whole or in part to define the three-dimensional structure of thecomplex.
 12. A method of identifying a ligand or low molecular weightcompound that binds to the catalytic domain of ZAP-70 kinase comprisingthe steps of: (i) using the three dimensional structure of the catalyticdomain of ZAP-70 kinase derived in whole or in part from the set ofatomic coordinates in Table 1 to select a potential ligand or lowmolecular weight compound that binds to the catalytic domain of ZAP-70(ii) selecting those ligands or low molecular weight compounds that bindto the catalytic domain of ZAP-70.
 13. A method of identifying a ligandor low molecular weight compound that binds to the catalytic domain ofZAP-70 kinase according to claim 11 wherein the catalytic domain ofZAP-70 kinase comprises at least the ATP-binding site of said domain.14. A method of claim 12 for use in selecting ligands which inhibit thebiological activity of ZAP-70 kinase.
 15. A method of designing a ligandor low molecular weight compound capable of binding to ZAP-70 catalyticdomain comprising: (i) using the atomic coordinates of Table 1 in wholeor in part to determine the three dimensional structure of ZAP-70catalytic domain (ii) probing the said catalytic domain of ZAP-70 with acandidate ligands or low molecular weight compounds to determine whichbind to the catalytic domain of ZAP-70 (iii) selecting those ligands orlow molecular weight compounds which bind to the catalytic domain ofZAP-70 (iv) modifying those ligands or low molecular weight compoundswhich bind to maximize physical binding properties such as Volubility,affinity, specificity or potency.
 16. A method according to claim 15wherein the candidate ligands or low molecular weight compounds arescreened in silica.
 17. A method according to claims 15 for use indesigning ligands which inhibit the biological activity of ZAP-70kinase.
 18. A pharmaceutical composition comprising a ligand identifiedby the methods of claim 12 for use of treatment of diseases andconditions involving T-cell and lymphocyte activation.